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Conserved domains on  [gi|648216203|ref|NP_001280244|]
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mannose-1-phosphate guanyltransferase beta [Gallus gallus]

Protein Classification

mannose-1-phosphate guanyltransferase( domain architecture ID 10157656)

mannose-1-phosphate guanyltransferase catalyzes the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids; similar to Homo sapiens mannose-1-phosphate guanyltransferase beta

EC:  2.7.7.13
Gene Ontology:  GO:0004475|GO:0009298|GO:0006486|GO:0005525

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-233 2.85e-163

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


:

Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 455.52  E-value: 2.85e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIRISLSHE 80
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLAEGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDSGRICRFV 160
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 161 EKPRVFVSNKINAGLYIFSPGILQRIQLRPTSIEKEIFPAMAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYL 233
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 255-334 1.22e-36

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd05824:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 80  Bit Score: 127.27  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 255 LVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIVND 334
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
 
Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-233 2.85e-163

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 455.52  E-value: 2.85e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIRISLSHE 80
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLAEGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDSGRICRFV 160
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 161 EKPRVFVSNKINAGLYIFSPGILQRIQLRPTSIEKEIFPAMAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYL 233
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-234 8.01e-88

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 264.32  E-value: 8.01e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEqRLGIRISLSHEK 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  82 EPLGTAGPLALARDLLaeGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDsGRICRFVE 161
Cdd:COG1208   80 EPLGTGGALKRALPLL--GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648216203 162 KPRVFVSNKINAGLYIFSPGILQRIQLRPT-SIEkEIFPAMAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYLQ 234
Cdd:COG1208  157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-315 1.90e-62

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 204.37  E-value: 1.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMrEQEQRLGIRISLSHE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYF-GDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   81 KEPLGTAGPLALARDLLAeggEPFFVLNSDVICEFPfaALARFHRQHggEGSIVVTRVEEPAKYGVVVSepDSGRICRFV 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD---DEFLVLNGDVLLDSD--LLERLIRAE--APAIAVVEVDDPSDYGVVET--DGGRVTGIV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  161 EKPRVFVSNKINAGLYIFSPGILQRIQLRPTSI--EKEIFPA---MAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYLQA 235
Cdd:TIGR03992 151 EKPENPPSNLINAGIYLFSPEIFELLEKTKLSPrgEYELTDAlqlLIDEGKVKAVELDGFWLDVGRPWDLLDANEALLDN 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  236 LRAQHPEKLHSGPGVVGNVLVDPSAK------------IGANCVIGPNVTIGAGVVVEDGVR------IKRCTVLQGARI 297
Cdd:TIGR03992 231 LEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNAYIRPYTVIGNNVHignaveIKNSIIMEGTKI 310

                         330
                  ....*....|....*...
gi 648216203  298 RSHSWLESCIVGWSCSVG 315
Cdd:TIGR03992 311 PHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-233 2.45e-62

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 199.40  E-value: 2.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKA-LLLHQLEALRQAGVSHVVLAVS-YMSEALEAAMREqEQRLGIRISLSH 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYpLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGD-GSKFGVQITYAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   80 EKEPLGTAGPLALARDLLAEGGEPFFVLNSDVICEFPFAALARFHRQHGGE--GSIVVTRVEEPAKYGVVVSEpDSGRIC 157
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFD-DNGRVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  158 RFVEKPRVFV-SNKINAGLYIFSPGILQRIQL------RPTSIEKEIFPAMAQDGQL-YAMELQGF-WMDIGQPKDFLTG 228
Cdd:pfam00483 159 RFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKyleelkRGEDEITDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEA 238


                  ....*
gi 648216203  229 MCMYL 233
Cdd:pfam00483 239 NLFLL 243
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 255-334 1.22e-36

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 127.27  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 255 LVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIVND 334
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-332 2.83e-20

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 91.71  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIrislshEKE 82
Cdd:PRK14356   8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVL------QEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGG-EPFFVLNSDVicefPF---AALARF-HRQHGGEGSIVVTRVEEPAKYGVVVSEpdSGRIC 157
Cdd:PRK14356  79 QLGTGHALQCAWPSLTAAGlDRVLVVNGDT----PLvttDTIDDFlKEAAGADLAFMTLTLPDPGAYGRVVRR--NGHVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 158 RFVE----KPRVF--VSNKINAGLYIFSPGILQRIQLRPTSIEKE--------IFPAMAQDGQLYAMELQGFW--MDIGQ 221
Cdd:PRK14356 153 AIVEakdyDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKSgeyyitdlVGLAVAEGMNVLGVNCGEDPnlLGVNT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 222 PKDfLTGMCMYLQALRA-QH---------PEKLHSGPGVVgnvlVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTV 291
Cdd:PRK14356 233 PAE-LVRSEELLRARIVeKHlesgvlihaPESVRIGPRAT----IEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVV 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 648216203 292 LQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIV 332
Cdd:PRK14356 308 SSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARV 348
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 232-329 2.23e-12

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 67.09  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 232 YLQALRAQHPEKLHSG-PGVVGNVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-KRCTVLQGARIRSHSWLES-CIV 308
Cdd:PRK00892  84 FARLAQLFDPPATPSPaAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGADCRLHAnVTI 163

                         90       100
                 ....*....|....*....|.
gi 648216203 309 GWSCSVGQWVRMENVTVLGED 329
Cdd:PRK00892 164 YHAVRIGNRVIIHSGAVIGSD 184
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 256-329 3.90e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 63.50  E-value: 3.90e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 256 VDPSAKIGANCVIGPNVTIGAGVVVEDGVRIK-RCTVLQGARIRSHSWLES-CIVGWSCSVGQWVRMENVTVLGED 329
Cdd:COG1044  105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHPnVTIYERCVIGDRVIIHSGAVIGAD 180
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
259-286 1.35e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.55  E-value: 1.35e-05
                          10        20
                  ....*....|....*....|....*...
gi 648216203  259 SAKIGANCVIGPNVTIGAGVVVEDGVRI 286
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 245-280 1.47e-03

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 39.40  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 648216203  245 HSGPGVV--GNVLVDPSAKIGANCVIGPNVTIGAGVVV 280
Cdd:TIGR03570 143 HIAPGVTlsGGVVIGEGVFIGAGATIIQGVTIGAGAIV 180
 
Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-233 2.85e-163

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 455.52  E-value: 2.85e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIRISLSHE 80
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLAEGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDSGRICRFV 160
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 161 EKPRVFVSNKINAGLYIFSPGILQRIQLRPTSIEKEIFPAMAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYL 233
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-234 8.01e-88

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 264.32  E-value: 8.01e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEqRLGIRISLSHEK 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  82 EPLGTAGPLALARDLLaeGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDsGRICRFVE 161
Cdd:COG1208   80 EPLGTGGALKRALPLL--GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648216203 162 KPRVFVSNKINAGLYIFSPGILQRIQLRPT-SIEkEIFPAMAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYLQ 234
Cdd:COG1208  157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-220 2.97e-83

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 252.12  E-value: 2.97e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEqRLGIRISLSHEKE 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGS-KFGVNIEYVVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLaeGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEpDSGRICRFVEK 162
Cdd:cd04181   80 PLGTAGAVRNAEDFL--GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELD-DDGRVTRFVEK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648216203 163 PRVFVSNKINAGLYIFSPGILQRIQLRPTS---IEKEIFPAMAQDGQLYAMELQGFWMDIG 220
Cdd:cd04181  157 PTLPESNLANAGIYIFEPEILDYIPEILPRgedELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-315 1.90e-62

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 204.37  E-value: 1.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMrEQEQRLGIRISLSHE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYF-GDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   81 KEPLGTAGPLALARDLLAeggEPFFVLNSDVICEFPfaALARFHRQHggEGSIVVTRVEEPAKYGVVVSepDSGRICRFV 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD---DEFLVLNGDVLLDSD--LLERLIRAE--APAIAVVEVDDPSDYGVVET--DGGRVTGIV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  161 EKPRVFVSNKINAGLYIFSPGILQRIQLRPTSI--EKEIFPA---MAQDGQLYAMELQGFWMDIGQPKDFLTGMCMYLQA 235
Cdd:TIGR03992 151 EKPENPPSNLINAGIYLFSPEIFELLEKTKLSPrgEYELTDAlqlLIDEGKVKAVELDGFWLDVGRPWDLLDANEALLDN 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  236 LRAQHPEKLHSGPGVVGNVLVDPSAK------------IGANCVIGPNVTIGAGVVVEDGVR------IKRCTVLQGARI 297
Cdd:TIGR03992 231 LEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNAYIRPYTVIGNNVHignaveIKNSIIMEGTKI 310

                         330
                  ....*....|....*...
gi 648216203  298 RSHSWLESCIVGWSCSVG 315
Cdd:TIGR03992 311 PHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-233 2.45e-62

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 199.40  E-value: 2.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKA-LLLHQLEALRQAGVSHVVLAVS-YMSEALEAAMREqEQRLGIRISLSH 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYpLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGD-GSKFGVQITYAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   80 EKEPLGTAGPLALARDLLAEGGEPFFVLNSDVICEFPFAALARFHRQHGGE--GSIVVTRVEEPAKYGVVVSEpDSGRIC 157
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFD-DNGRVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  158 RFVEKPRVFV-SNKINAGLYIFSPGILQRIQL------RPTSIEKEIFPAMAQDGQL-YAMELQGF-WMDIGQPKDFLTG 228
Cdd:pfam00483 159 RFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKyleelkRGEDEITDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEA 238


                  ....*
gi 648216203  229 MCMYL 233
Cdd:pfam00483 239 NLFLL 243
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-225 1.77e-60

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 193.92  E-value: 1.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEqRLGIRISLSHEKE 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGY-RGGIRIYYVIEPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEggEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEpDSGRICRFVEK 162
Cdd:cd06915   80 PLGTGGAIKNALPKLPE--DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVD-GDGRVIAFVEK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 163 PRVFVSNKINAGLYIFSPGILQRIQLRPTSIEKEIFPAMAQDGQLYAMELQGFWMDIGQPKDF 225
Cdd:cd06915  157 GPGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDY 219
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-227 6.97e-59

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 189.70  E-value: 6.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMReqEQRLGIRISLSHE- 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLG--DSRFGLRITISDEp 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLaeGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAK--YGVVVSEPDsGRICR 158
Cdd:cd06422   79 DELLETGGGIKKALPLL--GDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHngVGDFSLDAD-GRLRR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648216203 159 fveKPRVFVSNKINAGLYIFSPGILQRIQLRPTSIeKEIFPAMAQDGQLYAMELQGFWMDIGQPKDFLT 227
Cdd:cd06422  156 ---GGGGAVAPFTFTGIQILSPELFAGIPPGKFSL-NPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-219 9.99e-55

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 180.14  E-value: 9.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGG--FGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQ-AGVSHVVLAVSYMSEALEAAMREQEQRLGIRISLSH 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  80 EKEPLGTAGPLALARDLLAEGG-EPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPA--KYGVVVSEPDSGRI 156
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQILAGNpSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQasNYGCIVEDPSTGEV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 157 CRFVEKPRVFVSNKINAGLYIFSPGILQRIQL---------------------RPTSIEKEIFPAMAQDGQLYAMELQGF 215
Cdd:cd06428  161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKafqsrqqeaqlgddnnregraEVIRLEQDVLTPLAGSGKLYVYKTDDF 240


                 ....
gi 648216203 216 WMDI 219
Cdd:cd06428  241 WSQI 244
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-226 1.86e-51

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 171.21  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEqRLGIRISLSHE 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGS-RFGVRITYILQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLaeGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVsePDSGRICRFV 160
Cdd:cd04189   80 EEPLGLAHAVLAARDFL--GDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAV--VDDGRIVRLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648216203 161 EKPRVFVSNKINAGLYIFSPGILQRI-QLRPTSI-EKEIFPAM----AQDGQLYAMELQGFWMDIGQPKDFL 226
Cdd:cd04189  156 EKPKEPPSNLALVGVYAFTPAIFDAIsRLKPSWRgELEITDAIqwliDRGRRVGYSIVTGWWKDTGTPEDLL 227
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-225 7.53e-50

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 166.53  E-value: 7.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREqEQRLGIRISLSHEKE 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGD-GSKFGVNISYVREDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLaegGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVT--RVEEPakYGVVvsEPDSGRICRFV 160
Cdd:cd06426   80 PLGTAGALSLLPEKP---TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVReyEVQVP--YGVV--ETEGGRITSIE 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 161 EKPRvfVSNKINAGLYIFSPGILQRIQLR-----PTSIEKEIfpamAQDGQLYAMELQGFWMDIGQPKDF 225
Cdd:cd06426  153 EKPT--HSFLVNAGIYVLEPEVLDLIPKNeffdmPDLIEKLI----KEGKKVGVFPIHEYWLDIGRPEDY 216
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-309 1.72e-47

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 164.50  E-value: 1.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMS-EALEAAMREQEqRLGIRISLSHE 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTgEEIKEIVGEGE-RFGAKITYIVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   81 KEPLGTAGPLALARDLLaeGGEPFFVLNSDVICEF---PFaaLARFHRQHgGEGSIVVTRVEEPAKYGVVVSEpDSGRIC 157
Cdd:TIGR01208  80 GEPLGLAHAVYTARDFL--GDDDFVVYLGDNLIQDgisRF--VKSFEEKD-YDALILLTKVRDPTAFGVAVLE-DGKRIL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  158 RFVEKPRVFVSNKINAGLYIFSPGILQRIQLRPTSI--EKEIFPA---MAQDGQ-LYAMELQGFWMDIGQPKDFLTGMCM 231
Cdd:TIGR01208 154 KLVEKPKEPPSNLAVVGLYMFRPLIFEAIKNIKPSWrgELEITDAiqwLIEKGYkVGGSKVTGWWKDTGKPEDLLDANRL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  232 YL-QALRAQHPEKLHSgpGVVGNVLVDPSAK-----------IGANCVI-----GPNVTIGAGVVVEDGvRIKRCTVLQG 294
Cdd:TIGR01208 234 ILdEVEREVQGVDDES--KIRGRVVVGEGAKivnsvirgpavIGEDCIIensyiGPYTSIGEGVVIRDA-EVEHSIVLDE 310

                         330
                  ....*....|....*.
gi 648216203  295 ARIRS-HSWLESCIVG 309
Cdd:TIGR01208 311 SVIEGvQARIVDSVIG 326
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 2.49e-39

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 141.00  E-value: 2.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVS-YMSEALEAAMREQEQrLGIRISLSH 79
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGSQ-LGIKISYAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  80 EKEPLGTAGPLALARDLLaeGGEPFFVLNSDVICEFP-FAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDsGRICR 158
Cdd:COG1209   80 QPEPLGLAHAFIIAEDFI--GGDPVALVLGDNIFYGDgLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRVVS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 159 FVEKPRVFVSNKINAGLYIFSPGILQRIQ-LRPtSI--EKEI---FPAMAQDGQLY-AMELQGF-WMDIGQPKDFL-TGm 229
Cdd:COG1209  157 LEEKPKEPKSNLAVTGLYFYDNDVVEIAKnLKP-SArgELEItdaNQAYLERGKLVvELLGRGFaWLDTGTHESLLeAN- 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648216203 230 cMYLQALRAQHPEKLHSgPGVV----GNVLVDPSAKIG---ANCVIGPNVtigAGVVVEDGVRIK 287
Cdd:COG1209  235 -RFVLTIEKRQGLKIAC-PEEIayrmGWIDAEQLAKLAnslEKSGYGPYL---LRLLDSNRARVK 294
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 255-334 1.22e-36

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 127.27  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 255 LVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIVND 334
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-225 3.70e-30

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 115.34  E-value: 3.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMreQEQRLGIRISLSHEK 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL--ARPGPDVTFVYNPDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  82 EPLGTAGPLALARDLLaegGEPFFVLNSDVIceFPFAALARFHRqhgGEGSIVV---TRVEEPAKYGVVVSEPDSGRICR 158
Cdd:COG1213   79 DETNNIYSLWLAREAL---DEDFLLLNGDVV--FDPAILKRLLA---SDGDIVLlvdRKWEKPLDEEVKVRVDEDGRIVE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 159 FVEKPRvfvSNKINA---GLYIFSPGILQRIQLRPTSIEKEIFP----------AMAQDGQLYAMELQG-FWMDIGQPKD 224
Cdd:COG1213  151 IGKKLP---PEEADGeyiGIFKFSAEGAAALREALEALIDEGGPnlyyedalqeLIDEGGPVKAVDIGGlPWVEIDTPED 227


                 .
gi 648216203 225 F 225
Cdd:COG1213  228 L 228
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-330 1.33e-29

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 118.21  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQeqrlgiRISLSHEKE 82
Cdd:COG1207    5 VVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL------DVEFVLQEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGGEPFFVLNSDVicefPF------AALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDsGRI 156
Cdd:COG1207   76 QLGTGHAVQQALPALPGDDGTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDED-GRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 157 CRFVE----KPRVFVSNKINAGLYIFSPGILQRI--QLRPTSIEKE-----IFPAMAQDGQL-YAMELQGFWMDIG---- 220
Cdd:COG1207  151 LRIVEekdaTEEQRAIREINTGIYAFDAAALREAlpKLSNDNAQGEyyltdVIAIARADGLKvAAVQPEDPWEVLGvndr 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 221 -QpkdfLTGMCMYLQALRAQHpeklHSGPGVV----GNVLVDPSAKIGANCVIGPNV------TIGAGVVVEDGVRIKRC 289
Cdd:COG1207  231 vQ----LAEAERILQRRIAER----LMRAGVTiidpATTYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTLKDS 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 648216203 290 TVLQGARIRsHSWLESCIVGWSCSVGQWVRMENVTVLGEDV 330
Cdd:COG1207  303 TIGDGVVIK-YSVIEDAVVGAGATVGPFARLRPGTVLGEGV 342
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-329 1.52e-29

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 116.71  E-value: 1.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNK------AL--LLHqlealrqAGVSHVVLAVSYMSEALEAAMRE-QEQRL-- 71
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGKyriidfPLsnCVN-------SGIRRVGVLTQYKSHSLNDHIGSgKPWDLdr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  72 ---GIRI-----SLSHEKEPLGTAGPLALARDLLAEGGEPFF-VLNSDVICEFPFAALARFHRQHGGEGSIVVTRV--EE 140
Cdd:COG0448   77 krgGVFIlppyqQREGEDWYQGTADAVYQNLDFIERSDPDYVlILSGDHIYKMDYRQMLDFHIESGADITVACIEVprEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 141 PAKYGVVVSEPDsGRICRFVEKPRVFVSNKINAGLYIFSPGILQRI--QLRPTSIE---KEIFPAMAQDGQLYAMELQGF 215
Cdd:COG0448  157 ASRFGVMEVDED-GRITEFEEKPKDPKSALASMGIYVFNKDVLIELleEDAPNSSHdfgKDIIPRLLDRGKVYAYEFDGY 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 216 WMDIGQPKDfltgmcmYLQA---LRAQHPE------------KLHSGP-------GVVGNVLVDPSAKIGA---NCVIGP 270
Cdd:COG0448  236 WRDVGTIDS-------YYEAnmdLLDPEPEfnlydpewpiytKQKDLPpakfvrgGKVKNSLVSNGCIISGtveNSVLFR 308

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 648216203 271 NVTIGAGVVVEDGVrikrctVLQGARIRSHSWLESCIVGWSCSVGqwvrmENVtVLGED 329
Cdd:COG0448  309 GVRVESGAVVENSV------IMPGVVIGEGAVIENAIIDKNVVIP-----PGV-VIGED 355
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-225 2.25e-29

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 113.10  E-value: 2.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMreqEQRLGIRISLSHEKE 82
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL---KKYPNIKFVYNPDYA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLaegGEPFFVLNSDVICEfpfAALARFHRQHGGEGSIVVTRVEEPakYGVVVSEPDSGRICRFVEK 162
Cdd:cd02523   78 ETNNIYSLYLARDFL---DEDFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKE--WEDEYVKDLDDAGVLLGII 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 163 PRVFVSNKINA---GLYIFSPGILQRI-----QLRPTSIEK----EIFPAMAQDGQLYAMELQ-GFWMDIGQPKDF 225
Cdd:cd02523  150 SKAKNLEEIQGeyvGISKFSPEDADRLaealeELIEAGRVNlyyeDALQRLISEEGVKVKDISdGFWYEIDDLEDL 225
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-230 2.58e-29

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 113.44  E-value: 2.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEAL-EAAMREQEQRLGIRISLS--- 78
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIkEYFLNYFLHNSDVTIDLGtnr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  79 ---HEKEPLG-------------TAGPLALARDLLaEGGEPFFVLNSDVICEFPFAALARFHRQHGGegSIVVTRVEEPA 142
Cdd:cd02524   81 ielHNSDIEDwkvtlvdtglntmTGGRLKRVRRYL-GDDETFMLTYGDGVSDVNINALIEFHRSHGK--LATVTAVHPPG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 143 KYGVVVSEPDsGRICRFVEKPRVfVSNKINAGLYIFSPGILQRIQLRPTSIEKEIFPAMAQDGQLYAMELQGFW--MDIG 220
Cdd:cd02524  158 RFGELDLDDD-GQVTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWqcMDTL 235

                        250
                 ....*....|
gi 648216203 221 QPKDFLTGMC 230
Cdd:cd02524  236 RDKQTLEELW 245
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-226 1.01e-24

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 101.46  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPK---PLVefcNKALLLHQLEALRQAGVSHVVLAVSY----------MSEALEAAMREQ 67
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKemlPIV---DKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdRSYELEETLEKK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  68 -------EQR---LGIRISLSHEKEPLGTAGPLALARDLLaeGGEPFFVLNSDVIC---EFPFAALARFHRQHGgeGSIV 134
Cdd:cd02541   78 gktdlleEVRiisDLANIHYVRQKEPLGLGHAVLCAKPFI--GDEPFAVLLGDDLIdskEPCLKQLIEAYEKTG--ASVI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 135 -VTRV--EEPAKYGVVVSEPDSG---RICRFVEKPRVFV--SNKINAGLYIFSPGILQRIQLRPTSIEKEI-----FPAM 201
Cdd:cd02541  154 aVEEVppEDVSKYGIVKGEKIDGdvfKVKGLVEKPKPEEapSNLAIVGRYVLTPDIFDILENTKPGKGGEIqltdaIAKL 233

                        250       260
                 ....*....|....*....|....*
gi 648216203 202 AQDGQLYAMELQGFWMDIGQPKDFL 226
Cdd:cd02541  234 LEEEPVYAYVFEGKRYDCGNKLGYL 258
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-185 1.28e-21

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 91.81  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREqeqrlgIRISLSHEKE 82
Cdd:cd02540    1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN------PNVEFVLQEE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGGEPFFVLNSDVicefPF------AALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEpDSGRI 156
Cdd:cd02540   72 QLGTGHAVKQALPALKDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVLTAELEDPTGYGRIIRD-GNGKV 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 648216203 157 CRFVE---------KPRVfvsnkINAGLYIFSPGILQR 185
Cdd:cd02540  147 LRIVEekdateeekAIRE-----VNAGIYAFDAEFLFE 179
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-332 2.83e-20

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 91.71  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIrislshEKE 82
Cdd:PRK14356   8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVL------QEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGG-EPFFVLNSDVicefPF---AALARF-HRQHGGEGSIVVTRVEEPAKYGVVVSEpdSGRIC 157
Cdd:PRK14356  79 QLGTGHALQCAWPSLTAAGlDRVLVVNGDT----PLvttDTIDDFlKEAAGADLAFMTLTLPDPGAYGRVVRR--NGHVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 158 RFVE----KPRVF--VSNKINAGLYIFSPGILQRIQLRPTSIEKE--------IFPAMAQDGQLYAMELQGFW--MDIGQ 221
Cdd:PRK14356 153 AIVEakdyDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKSgeyyitdlVGLAVAEGMNVLGVNCGEDPnlLGVNT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 222 PKDfLTGMCMYLQALRA-QH---------PEKLHSGPGVVgnvlVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTV 291
Cdd:PRK14356 233 PAE-LVRSEELLRARIVeKHlesgvlihaPESVRIGPRAT----IEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVV 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 648216203 292 LQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIV 332
Cdd:PRK14356 308 SSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARV 348
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-330 4.51e-19

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 87.88  E-value: 4.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQrlgirISLSHEKE 82
Cdd:PRK14355   6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGGEPFFVLNSDV--ICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDsGRICRFV 160
Cdd:PRK14355  78 QLGTGHAVACAAPALDGFSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDAD-GRVLRIV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 161 EK----PRVFVSNKINAGLYIFSPGILQRI--QLRPTSIEKE-----IFPAMAQDGQLY-------AMELQGFwMDIGQp 222
Cdd:PRK14355 157 EEkdatPEERSIREVNSGIYCVEAAFLFDAigRLGNDNAQGEyyltdIVAMAAAEGLRClafpvadPDEIMGV-NDRAQ- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 223 kdfltgMCMYLQALRAQHPEKLHsgpgVVGNVLVDPSA-------KIGANCVIGPNVT------IGAGVVVEDGVRIKRC 289
Cdd:PRK14355 235 ------LAEAARVLRRRINRELM----LAGVTLIDPETtyidrgvVIGRDTTIYPGVCisgdtrIGEGCTIEQGVVIKGC 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 648216203 290 TVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDV 330
Cdd:PRK14355 305 RIGDDVTVKAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHV 345
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-334 1.26e-18

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 86.81  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEaleaamrEQEQRLGIRISLSHEKE 82
Cdd:PRK14354   5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAE-------EVKEVLGDRSEFALQEE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGGEPFFVLNSDV--ICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEpDSGRICRFV 160
Cdd:PRK14354  75 QLGTGHAVMQAEEFLADKEGTTLVICGDTplITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRN-ENGEVEKIV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 161 EKP-------RVfvsNKINAGLYIFSPGILqriqlrptsIE--KEIFPAMAQdGQLY---AMEL---QGFWMDIGQPKDF 225
Cdd:PRK14354 154 EQKdateeekQI---KEINTGTYCFDNKAL---------FEalKKISNDNAQ-GEYYltdVIEIlknEGEKVGAYQTEDF 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 226 LTGM-----CMYLQA---LRAQHPEKlHSGPGVV----GNVLVDPSAKIGANCVIGPNV------TIGAGVVVEDGVRIK 287
Cdd:PRK14354 221 EESLgvndrVALAEAekvMRRRINEK-HMVNGVTiidpESTYIDADVEIGSDTVIEPGVvikgntVIGEDCVIGPGSRIV 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 648216203 288 RCTVLQGARIRsHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIVND 334
Cdd:PRK14354 300 DSTIGDGVTIT-NSVIEESKVGDNVTVGPFAHLRPGSVIGEEVKIGN 345
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-332 1.22e-17

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 83.76  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMReqeqRLGIRISLSHEKE 82
Cdd:PRK14353   8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAA----KIAPDAEIFVQKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALARDLLAEGGEPFFVLNSDVicefPF---AALARFhRQHGGEGSIVV---TRVEEPAKYGVVVSEPdsGRI 156
Cdd:PRK14353  81 RLGTAHAVLAAREALAGGYGDVLVLYGDT----PLitaETLARL-RERLADGADVVvlgFRAADPTGYGRLIVKG--GRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 157 CRFVE-KPRVFVSNKI---NAGLYIFSPGILQRI--QLRPTSIEKEIF------PAMAQDGQLYAMELqgfwmdigqPKD 224
Cdd:PRK14353 154 VAIVEeKDASDEERAItlcNSGVMAADGADALALldRVGNDNAKGEYYltdivaIARAEGLRVAVVEA---------PED 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 225 FLTGM--CMYLQALRAQHPEKLHSGPGVVGNVLVDPSA-------KIGANCVIGPNVTIGAGVVVEDgvrikrctvlqGA 295
Cdd:PRK14353 225 EVRGInsRAELAEAEAVWQARRRRAAMLAGVTLIAPETvffsydtVIGRDVVIEPNVVFGPGVTVAS-----------GA 293

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 648216203 296 RIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIV 332
Cdd:PRK14353 294 VIHAFSHLEGAHVGEGAEVGPYARLRPGAELGEGAKV 330
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 255-334 1.37e-17

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 76.51  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 255 LVDPSAKIGANCVIGPNVtIGAGVVVEDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDVIVND 334
Cdd:cd03356    1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-179 5.33e-17

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 78.83  E-value: 5.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMRE---QEQRLGIRIS--L 77
Cdd:cd02507    3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKskwSSLSSKMIVDviT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  78 SHEKEPLGTAgplalARDLLAEGGEP--FFVLNSDVICEFPFA-ALARFHRQHGGEGSIVVTRVEEPakygvvvsePDSG 154
Cdd:cd02507   83 SDLCESAGDA-----LRLRDIRGLIRsdFLLLSCDLVSNIPLSeLLEERRKKDKNAIATLTVLLASP---------PVST 148

                        170       180
                 ....*....|....*....|....*.
gi 648216203 155 RICRFVEKPRVF-VSNKINAGLYIFS 179
Cdd:cd02507  149 EQSKKTEEEDVIaVDSKTQRLLLLHY 174
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-330 9.19e-17

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 81.18  E-value: 9.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMReqeqrlGIRISLSHE 80
Cdd:PRK14358   8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ------GSGVAFARQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLAEGGEPFFVLNSDVICEFP--FAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDsGRICR 158
Cdd:PRK14358  79 EQQLGTGDAFLSGASALTEGDADILVLYGDTPLLRPdtLRALVADHRAQGSAMTILTGELPDATGYGRIVRGAD-GAVER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 159 FVEKPRVFVSNK----INAGLYIF---SPGILQRIqlrpTSIEKEifpamaqdGQLYAMELQGFWMDIG---------QP 222
Cdd:PRK14358 158 IVEQKDATDAEKaigeFNSGVYVFdarAPELARRI----GNDNKA--------GEYYLTDLLGLYRAGGaqvrafklsDP 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 223 KDFL-----TGMCMyLQALRAQHPEKLHSGPGVV----GNVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVL- 292
Cdd:PRK14358 226 DEVLgandrAGLAQ-LEATLRRRINEAHMKAGVTlqdpGTILIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVt 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 648216203 293 -----QGARIRSHSWLESCIVGWSCSVGQWVRMENVTVLGEDV 330
Cdd:PRK14358 305 dsvlhEGAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGV 347
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-298 5.42e-15

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 75.63  E-value: 5.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLH-QLEALRQAGVSHVVLAVSYMSEALEAAMREQ-------------- 67
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDfVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTwrlsgllgnyitpv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  68 --EQRLGIRISLshekeplGTAGplALARDL-LAEGGEP--FFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRV--EE 140
Cdd:PRK00844  88 paQQRLGKRWYL-------GSAD--AIYQSLnLIEDEDPdyVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVprEE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 141 PAKYGVVVSEPDsGRICRFVEKP-----------RVFVSnkinAGLYIFSPGIL----QRIQLRPTSIE---KEIFPAMA 202
Cdd:PRK00844 159 ASAFGVIEVDPD-GRIRGFLEKPadppglpddpdEALAS----MGNYVFTTDALvdalRRDAADEDSSHdmgGDIIPRLV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 203 QDGQLYAM------------ELQGFWMDIG---------------QPKdfltgMCMYLQA--LRAQH----PEK-LHSGP 248
Cdd:PRK00844 234 ERGRAYVYdfstnevpgateRDRGYWRDVGtidayydahmdllsvHPV-----FNLYNREwpIYTSSpnlpPAKfVDGGG 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648216203 249 GVVG--NVLVDPSAKI-GA---NCVIGPNVTIGAGVVVE-----DGVRIKRctvlqGARIR 298
Cdd:PRK00844 309 RVGSaqDSLVSAGSIIsGAtvrNSVLSPNVVVESGAEVEdsvlmDGVRIGR-----GAVVR 364
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-226 2.50e-14

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 71.84  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVsHVVLAVSymseALEAAMREQE-----QRLGIRI 75
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGI-REILIIS----TPEDLPLFKEllgdgSDLGIRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  76 SLSHEKEPLGTAGPLALARDLLaeGGEPFFVLNSDVICEFPF--AALARFHRQHGGeGSIVVTRVEEPAKYGVVvsEPD- 152
Cdd:cd02538   76 TYAVQPKPGGLAQAFIIGEEFI--GDDPVCLILGDNIFYGQGlsPILQRAAAQKEG-ATVFGYEVNDPERYGVV--EFDe 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 153 SGRICRFVEKPRVFVSNKINAGLYIFSPGILQRI-QLRPTSI-EKEIFP---AMAQDGQLYA--MELQGFWMDIGQPKDF 225
Cdd:cd02538  151 NGRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAkQLKPSARgELEITDvnnEYLEKGKLSVelLGRGFAWLDTGTHESL 230


                 .
gi 648216203 226 L 226
Cdd:cd02538  231 L 231
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-332 3.13e-14

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 72.98  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLH-QLEALRQAGVSHVVLAVSYMSEALEAamreqeqRLGI------ 73
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDfTLSNCANSGIDTVGVLTQYQPLELNN-------HIGIgspwdl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  74 -RI-----------SLSHEKEPLGTAGPLALARDLLaEGGEPFFV--LNSDVICEFPFAALARFHRQHGGEGSIVVTRV- 138
Cdd:PRK05293  77 dRInggvtilppysESEGGKWYKGTAHAIYQNIDYI-DQYDPEYVliLSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVp 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 139 -EEPAKYGVVVSEPDsGRICRFVEKPRVFVSNKINAGLYIFSPGILQRIQLR----PTSIE---KEIFPAMAQDG-QLYA 209
Cdd:PRK05293 156 wEEASRFGIMNTDEN-MRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYLIEdeknPNSSHdfgKNVIPLYLEEGeKLYA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 210 MELQGFWMDIGQPKDfltgmcmYLQA---LRAQHPE--------KLHS----------GPGV-VGNVLVDPSAKI-GA-- 264
Cdd:PRK05293 235 YPFKGYWKDVGTIES-------LWEAnmeLLRPENPlnlfdrnwRIYSvnpnlppqyiAENAkVKNSLVVEGCVVyGTve 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648216203 265 NCVIGPNVTIGAGVVVEDGVrikrctVLQGARIRSHSWLESCIVGWSCSVGQWVRM----ENVTVLGEDVIV 332
Cdd:PRK05293 308 HSVLFQGVQVGEGSVVKDSV------IMPGAKIGENVVIERAIIGENAVIGDGVIIgggkEVITVIGENEVI 373
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-338 1.12e-13

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 71.88  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   5 ILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMR--------EQEQRLG---- 72
Cdd:PRK14360   6 ILAAGKGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAhlpglefvEQQPQLGtgha 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  73 IRISLSHEKEPLGtagplalarDLLaeggepffVLNSDV--ICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSE 150
Cdd:PRK14360  83 VQQLLPVLKGFEG---------DLL--------VLNGDVplLRPETLEALLNTHRSSNADVTLLTARLPNPKGYGRVFCD 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 151 PDsGRICRFVEK----PRVFVSNKINAGLYIFSPGILQRI--QLRPTSIEKEIF---------PAMAQD--------G-- 205
Cdd:PRK14360 146 GN-NLVEQIVEDrdctPAQRQNNRINAGIYCFNWPALAEVlpKLSSNNDQKEYYltdtvslldPVMAVEvedyqeinGin 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 206 ---QLYAME------LQGFWMDIGqpkdfltgmCMYLQALRAQHPEKLHSGPGVVgnvlVDPSAKIGANCVIGPNVTIGA 276
Cdd:PRK14360 225 drkQLAQCEeilqnrIKEKWMLAG---------VTFIDPASCTISETVELGPDVI----IEPQTHLRGNTVIGSGCRIGP 291

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 277 GVVVEDGVRIKRCTVLQ----GARIRSHSWL-------ESCIVGWSCSVGQWVRMENvTVLGEDVIVNDELYL 338
Cdd:PRK14360 292 GSLIENSQIGENVTVLYsvvsDSQIGDGVKIgpyahlrPEAQIGSNCRIGNFVEIKK-SQLGEGSKVNHLSYI 363
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-330 1.40e-13

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 71.33  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRpltlSR-PKPLVEFCNKALLLHQLEALRQAGvSHVVLAVSYMSEALEAAMREQeqrlgirISLSH 79
Cdd:PRK14357   1 MRALVLAAGKGTRMK----SKiPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEW-------VKIFL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  80 EKEPLGTAGPLALARDLLAEGgEPFFVLNSDV--ICEFPFAALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPDSGRIC 157
Cdd:PRK14357  69 QEEQLGTAHAVMCARDFIEPG-DDLLILYGDVplISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYRIV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 158 RFVEKPRVFVSNK-INAGLYIFSPGILQRIQlrptsieKEIFPAMAQdGQLYAMELQGFWMDIGQPK----DFLTGMCMY 232
Cdd:PRK14357 148 EDKDAPEEEKKIKeINTGIYVFSGDFLLEVL-------PKIKNENAK-GEYYLTDAVNFAEKVRVVKtedlLEITGVNTR 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 233 LQ------ALRAQHPEKL-HSGPGVV--GNVLVDPSAKIGANCVIGP------NVTIGAGVVVEDGVRIKRCTVLQGARI 297
Cdd:PRK14357 220 IQlawlekQLRMRILEELmENGVTILdpNTTYIHYDVEIGMDTIIYPmtfiegKTRIGEDCEIGPMTRIVDCEIGNNVKI 299

                        330       340       350
                 ....*....|....*....|....*....|...
gi 648216203 298 rSHSWLESCIVGWSCSVGQWVRMENVTVLGEDV 330
Cdd:PRK14357 300 -IRSECEKSVIEDDVSVGPFSRLREGTVLKKSV 331
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-127 2.98e-13

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 68.07  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEA-LEAAMREQEQRLGIRIS--L 77
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAeISTYLRSFPLNLKQKLDevT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 648216203  78 SHEKEPLGTAGPLalaRDLLAEGGEPFFVLNSDVICEFPFAALARFHRQH 127
Cdd:cd04198   81 IVLDEDMGTADSL---RHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSH 127
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 253-330 3.18e-13

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 67.45  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 253 NVLVDPSAKIGANCVIGPNV------TIGAGVVVEDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVL 326
Cdd:cd03353    9 TTYIDGDVEIGVDVVIDPGVilegktVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRPGTVL 88


                 ....
gi 648216203 327 GEDV 330
Cdd:cd03353   89 GEGV 92
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 232-329 2.23e-12

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 67.09  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 232 YLQALRAQHPEKLHSG-PGVVGNVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-KRCTVLQGARIRSHSWLES-CIV 308
Cdd:PRK00892  84 FARLAQLFDPPATPSPaAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGADCRLHAnVTI 163

                         90       100
                 ....*....|....*....|.
gi 648216203 309 GWSCSVGQWVRMENVTVLGED 329
Cdd:PRK00892 164 YHAVRIGNRVIIHSGAVIGSD 184
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 256-329 3.90e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 63.50  E-value: 3.90e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 256 VDPSAKIGANCVIGPNVTIGAGVVVEDGVRIK-RCTVLQGARIRSHSWLES-CIVGWSCSVGQWVRMENVTVLGED 329
Cdd:COG1044  105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHPnVTIYERCVIGDRVIIHSGAVIGAD 180
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 238-342 8.10e-11

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 60.88  E-value: 8.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 238 AQHPEKLHSGPGVVgnvlVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIK-RCTVLQGARIRSHswlesCIVGWSCSVGQ 316
Cdd:cd03352    2 AKIGENVSIGPNAV----IGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHpNVTIYEGCIIGDR-----VIIHSGAVIGS 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648216203 317 -----------WVRMENV--TVLGEDVIVndelylnGAN 342
Cdd:cd03352   73 dgfgfapdgggWVKIPQLggVIIGDDVEI-------GAN 104
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 253-342 1.66e-10

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 61.57  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 253 NVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-KRCTVLQGARIRSHSWL-ESCIVGWSCSVGQ------------WV 318
Cdd:COG1044  114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIgDDCVLHPNVTIYERCVIgDRVIIHSGAVIGAdgfgfapdedggWV 193

                         90       100
                 ....*....|....*....|....*..
gi 648216203 319 RME---NVtVLGEDVivndELylnGAN 342
Cdd:COG1044  194 KIPqlgRV-VIGDDV----EI---GAN 212
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-329 2.59e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 61.49  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTlsrPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRlgIRISLshEKE 82
Cdd:PRK14352   7 VIVLAAGAGTRMRSDT---PKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPE--VDIAV--QDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  83 PLGTAGPLALArdlLAEGGEPF----FVLNSDVicefPF------AALARFHRQHGGEGSIVVTRVEEPAKYGVVVSEPD 152
Cdd:PRK14352  80 QPGTGHAVQCA---LEALPADFdgtvVVTAGDV----PLldgetlADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 153 sGRICRFVEK----PRVFVSNKINAGLYIFSPGILQRIQLRPTSiekeifpAMAQdGQLYAMELQGFWMDIGQP------ 222
Cdd:PRK14352 153 -GEVTAIVEQkdatPSQRAIREVNSGVYAFDAAVLRSALARLSS-------DNAQ-GELYLTDVLAIAREAGHRvgahha 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 223 KD--FLTGMCMYLQ--ALRAQHPEKLHSGPGVVGNVLVDPS-------AKIGANCVIGPNV------TIGAGVVVEDGVR 285
Cdd:PRK14352 224 DDsaEVAGVNDRVQlaALGAELNRRIVEAWMRAGVTIVDPAttwidvdVTIGRDVVIHPGTqllgrtTIGEDAVVGPDTT 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 648216203 286 IKRCTVLQGAR-IRSHSwlESCIVGWSCSVGQWVRMENVTVLGED 329
Cdd:PRK14352 304 LTDVTVGEGASvVRTHG--SESEIGAGATVGPFTYLRPGTVLGEE 346
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 259-329 9.25e-10

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 57.80  E-value: 9.25e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 259 SAKIGANCVIGPNVTIGAGVVVEDGVRIK-RCTVLQGARIRSHSWLES-CIVGWSCSVGQWVRMENVTVLGED 329
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPnVTIYEGCIIGDRVIIHSGAVIGSD 73
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 256-332 1.82e-09

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 58.49  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 256 VDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRctvlqGARIRSHswlesCIVGWSCSVGQWVR-MENVTV-----LGED 329
Cdd:COG1044   99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGD-----GVVIGPG-----VVIGDGVVIGDDCVlHPNVTIyercvIGDR 168


                 ...
gi 648216203 330 VIV 332
Cdd:COG1044  169 VII 171
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-126 2.51e-09

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 56.85  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLG------IRIS 76
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPksslmiVIII 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648216203  77 LSHEKEPLGTAgplalARDLLAEGGE--PFFVLNSDVICEFPFAALARFHRQ 126
Cdd:cd04197   83 MSEDCRSLGDA-----LRDLDAKGLIrgDFILVSGDVVSNIDLKEILEEHKE 129
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-232 7.08e-09

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 56.44  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVL-------AV------SYMSEALEAAmREQ 67
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknAVenhfdtSYELESLLEQ-RVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  68 EQRL---------GIRISLSHEKEPLGTAGPLALARDLLaeGGEPFFVLNSDVICE--------FPFAAL-ARF------ 123
Cdd:PRK10122  83 RQLLaevqsicppGVTIMNVRQGQPLGLGHSILCARPAI--GDNPFVVVLPDVVIDdasadplrYNLAAMiARFnetgrs 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 124 ----HRQHGGEGSIVVTRVEEPakygvVVSEPDSGRICRFVEK---PRVFVSNKINAGLYIFS-----------PGILQR 185
Cdd:PRK10122 161 qvlaKRMPGDLSEYSVIQTKEP-----LDREGKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSadiwpelertePGAWGR 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 648216203 186 IQLRPTSIEkeifpaMAQDGQLYAMELQGFWMDIGQPKDFLTGMCMY 232
Cdd:PRK10122 236 IQLTDAIAE------LAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKY 276
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-208 7.19e-09

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 55.72  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   4 LILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSymSEALEAAMREQEQRLGIR----ISLSH 79
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR--DEHNTKFHLDESLKLLAPnatvVELDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  80 EKEplGTAGPLALARDLLaEGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIVVTRVEEPaKYGVVVSEpDSGRICRF 159
Cdd:cd04183   80 ETL--GAACTVLLAADLI-DNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLD-ENGRVIET 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 648216203 160 VEKPRvfVSNKINAGLYIFSPGILQRiqlrpTSIEKEIFPAMAQDGQLY 208
Cdd:cd04183  155 AEKEP--ISDLATAGLYYFKSGSLFV-----EAAKKMIRKDDSVNGEFY 196
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-308 8.87e-09

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 56.54  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   4 LILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQL-EALRQAGVSHVVLavSYMSEALEAAMREQEQrlGIRISLS-HEK 81
Cdd:PRK14359   6 IILAAGKGTRMKS---SLPKVLHTICGKPMLFYILkEAFAISDDVHVVL--HHQKERIKEAVLEYFP--GVIFHTQdLEN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  82 EPlGTAGplALARDLLAegGEPFFVLNSD--VICEfpfAALARFHRQHgGEGSIVVTRVEEPAKYGVVVSEpdSGRICRF 159
Cdd:PRK14359  79 YP-GTGG--ALMGIEPK--HERVLILNGDmpLVEK---DELEKLLEND-ADIVMSVFHLADPKGYGRVVIE--NGQVKKI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 160 VEKPRVFVSNK----INAGLYIFSPGILQRI--QLRPTSIEKE------IFPAMAQDGQLYAMEL-QGFWMDIGQPKDFL 226
Cdd:PRK14359 148 VEQKDANEEELkiksVNAGVYLFDRKLLEEYlpLLKNQNAQKEyyltdiIALAIEKGETIKAVFVdEENFMGVNSKFELA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 227 TGMCMYLQALRaQHPEKLhsgpGVVGN----VLVDPSAKIGANCVIgpnvtigagvvvEDGVRIKRCTVLQGARIRSHSW 302
Cdd:PRK14359 228 KAEEIMQERIK-KNAMKQ----GVIMRlpetIYIESGVEFEGECEL------------EEGVRILGKSKIENSHIKAHSV 290


                 ....*.
gi 648216203 303 LESCIV 308
Cdd:PRK14359 291 IEESII 296
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-220 9.29e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 55.84  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIRISLSHEK 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  82 EPLGTAGPLALARDLLAeGGEPFFVLNSDVIC--EFPFAALARFHRQHGgeGSIVVTRVEEPAKYGVVVSEpDSGRICRF 159
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIG-GDDCALVLGDNIFYghDLPKLMEAAVNKESG--ATVFAYHVNDPERYGVVEFD-QNGTAISL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648216203 160 VEKPRVFVSNKINAGLYIFSPGILQRIQ-LRPTSI-EKEIFPA----MAQDGQLYAMELQGF-WMDIG 220
Cdd:PRK15480 161 EEKPLQPKSNYAVTGLYFYDNDVVEMAKnLKPSARgELEITDInriyMEQGRLSVAMMGRGYaWLDTG 228
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 255-297 9.30e-09

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 55.41  E-value: 9.30e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 255 LVDPSAKIGAN------CVIGPNVTIGAG------VVVEDGVRI-KRCTVLQGARI 297
Cdd:COG1043    9 IVDPGAKLGENveigpfCVIGPDVEIGDGtvigshVVIEGPTTIgKNNRIFPFASI 64
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-220 1.55e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 56.00  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNK------AL--LLHQleALRQAGV----------SHVVLAVSYMS------- 57
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGKfriidfALsnCINS--GIRRIGVltqykahsliRHIQRGWSFFReelgefv 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  58 EALEAAMReqeqrlgirisLSHEKEPLGTAGPLALARDLL-AEGGEPFFVLNSDVICEFPFAALARFHRQHGGE---GSI 133
Cdd:PRK00725  96 DLLPAQQR-----------VDEENWYRGTADAVYQNLDIIrRYDPKYVVILAGDHIYKMDYSRMLADHVESGADctvACL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 134 VVTRvEEPAKYGVV-VSEpdSGRICRFVEKP-----------RVFVSnkinAGLYIFSPGILQRiQLR-----PTS---I 193
Cdd:PRK00725 165 EVPR-EEASAFGVMaVDE--NDRITAFVEKPanppampgdpdKSLAS----MGIYVFNADYLYE-LLEedaedPNSshdF 236

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 648216203 194 EKEIFPAMAQDGQLYA-----------MELQGFWMDIG 220
Cdd:PRK00725 237 GKDIIPKIVEEGKVYAhpfsdscvrsdPEEEPYWRDVG 274
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
255-297 3.44e-08

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 53.95  E-value: 3.44e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 255 LVDPSAKIGAN------CVIGPNVTIGAG------VVVEDGVRI-KRCTVLQGARI 297
Cdd:PRK05289  10 IVEPGAKIGENveigpfCVIGPNVVIGDGtvigshVVIDGHTTIgKNNRIFPFASI 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 255-297 4.06e-08

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 53.59  E-value: 4.06e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 255 LVDPSAKIGAN------CVIGPNVTIGAG------VVVEDGVRI-KRCTVLQGARI 297
Cdd:cd03351    7 IVDPGAKIGENveigpfCVIGPNVEIGDGtvigshVVIDGPTTIgKNNRIFPFASI 62
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-183 5.68e-08

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 53.35  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPltLSR---PKPLVE-FCNKALLLHQLEALRQAGVSHVVLAVSymSEALEAAMREQ--EQRLGIR 74
Cdd:cd02509    1 IYPVILAGGSGTRLWP--LSResyPKQFLKlFGDKSLLQQTLDRLKGLVPPDRILVVT--NEEYRFLVREQlpEGLPEEN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  75 ISLshekEPLG--TAGPLALA-RDLLAEGGEP-FFVLNSD-VIcefpfAALARFHR--QHGGE----GSIVVtrveepak 143
Cdd:cd02509   77 IIL----EPEGrnTAPAIALAaLYLAKRDPDAvLLVLPSDhLI-----EDVEAFLKavKKAVEaaeeGYLVT-------- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648216203 144 YGVVVSEPDSG---------------RICRFVEKP-----RVFVSNK---INAGLYIFSPGIL 183
Cdd:cd02509  140 FGIKPTRPETGygyieageklgggvyRVKRFVEKPdletaKEYLESGnylWNSGIFLFRAKTF 202
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-220 1.13e-07

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 52.39  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    2 RALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQEQRLGIRISLSHEK 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   82 EPLGTAGPLALARDLLaeGGEPF-FVLNSDVICEFPFA-ALARFHRQHGGeGSIVVTRVEEPAKYGVVvsEPDS-GRICR 158
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFI--GGDPSaLVLGDNIFYGHDLSdLLRRAAARTEG-ATVFAYQVSDPERYGVV--EFDSnGRAIS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648216203  159 FVEKPRVFVSNKINAGLYIFSPGILQ---------RIQLRPTSIEKEIFpamaQDGQLyAMEL--QGF-WMDIG 220
Cdd:TIGR01207 156 IEEKPAQPKSNYAVTGLYFYDNRVVEiarqlkpsaRGELEITDLNRVYL----EEGRL-SVELlgRGYaWLDTG 224
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-145 3.43e-07

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 49.50  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203    3 ALILVGGFGTRLRpltlsRPKPLVEFCNKALLLHQLEALRQAGvSHVVLAVSYmsEALEAAMReqeqRLGIRISLshekE 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALA----GLGVPVVP----D 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203   83 PLGTAGPL-----ALARdllAEGGEPFFVLNSDVicefPF------AALARFHRQHGGEGSIVVTRVE--EPAKYG 145
Cdd:pfam12804  65 PDPGQGPLagllaALRA---APGADAVLVLACDM----PFltpellRRLLAAAEESGADIVVPVYDGGrgHPLLYR 133
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-111 3.47e-07

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 49.89  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   8 GGFGTRLRpltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREqeqrLGIRIslsHEKEPLGTA 87
Cdd:COG2266    3 GGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKE----RGVEV---IETPGEGYV 71

                         90       100
                 ....*....|....*....|....
gi 648216203  88 GPLALArdlLAEGGEPFFVLNSDV 111
Cdd:COG2266   72 EDLNEA---LESISGPVLVVPADL 92
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-219 9.16e-07

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 48.69  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALLLH-QLEALRQAGVSHVVLAVSYMSEALEAAMREqeqrlGIRISLSHEK 81
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDfPLSNMVNSGIRNVGVLTQYKSRSLNDHLGS-----GKEWDLDRKN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  82 EPL---------------GTAGPLALARDLLAEGGEPFFV-LNSDVICEFPFAALARFHRQHGGEGSIVVtrveepakyg 145
Cdd:cd02508   76 GGLfilppqqrkggdwyrGTADAIYQNLDYIERSDPEYVLiLSGDHIYNMDYREMLDFHIESGADITVVY---------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 146 vvvsepdsgricrfvekprvfvsnKINAGLYIFSPGILqrIQL-----RPTSIE--KEIFPAMAQDGQLYAMELQGFWMD 218
Cdd:cd02508  146 ------------------------KASMGIYIFSKDLL--IELleedaADGSHDfgKDIIPAMLKKLKIYAYEFNGYWAD 199


                 .
gi 648216203 219 I 219
Cdd:cd02508  200 I 200
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-140 2.90e-06

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 47.19  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRlrpltLSRPKPLVEFCNKALLLHQLEALRQAgVSHVVLAVSymsealeaamREQEQ--RLGIRISls 78
Cdd:cd02503    1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLERLKPL-VDEVVISAN----------RDQERyaLLGVPVI-- 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203  79 heKEPLGTAGPLA-LARDLLAEGGEPFFVLNSDviceFPF---AALARFHRQHGGEGSIVVTRVEE 140
Cdd:cd02503   63 --PDEPPGKGPLAgILAALRAAPADWVLVLACD----MPFlppELLERLLAAAEEGADAVVPKSGG 122
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 255-333 8.89e-06

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 43.34  E-value: 8.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 255 LVDPSAKIGA-----NCVIGPNVTIGagvvveDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVTVlGED 329
Cdd:cd04652    1 LVGENTQVGEktsikRSVIGANCKIG------KRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLV-GSG 73


                 ....
gi 648216203 330 VIVN 333
Cdd:cd04652   74 YRVE 77
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 255-316 1.08e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 42.95  E-value: 1.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648216203 255 LVDPSAKIGANC-----VIGPNVTIGA-----------GVVVEDGVRIKRCTVLQGARIRSHSWLE-SCIVGWSCSVGQ 316
Cdd:cd05787    1 VIGRGTSIGEGTtiknsVIGRNCKIGKnvvidnsyiwdDVTIEDGCTIHHSIVADGAVIGKGCTIPpGSLISFGVVIGD 79
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
259-286 1.35e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.55  E-value: 1.35e-05
                          10        20
                  ....*....|....*....|....*...
gi 648216203  259 SAKIGANCVIGPNVTIGAGVVVEDGVRI 286
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-140 2.21e-05

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 44.41  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRpltlsRPKPLVEFCNKALLLHQLEALRQAgVSHVVLAVSYmsealeaamREQEQRLGIRIslshEKE 82
Cdd:COG0746    7 GVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR---------PERYAALGVPV----VPD 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648216203  83 PLGTAGPLA-LARDLLAEGGEPFFVLNSDVicefPF---AALARFHRQHGGEGSIVVTRVEE 140
Cdd:COG0746   68 DPPGAGPLAgILAALEAAPAEWVLVLACDM----PFlppDLVRRLLEALEEGADAVVPRSGG 125
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-220 2.46e-05

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 45.83  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPLtlSR---PKPLVEFCNKALLLhQLEALRQAGVSHV--VLAVSymSEALEAAMREQEQRLGI-R 74
Cdd:COG0836    3 IYPVILAGGSGTRLWPL--SResyPKQFLPLLGEKSLL-QQTVERLAGLVPPenILVVT--NEEHRFLVAEQLPELGPaN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  75 ISLshekEPLG--TAGPLALA-RDLLAEGGEP-FFVLNSD-VIcefpfAALARFHR------QHGGEGSIVV-----TRv 138
Cdd:COG0836   78 ILL----EPVGrnTAPAIALAaLLIAKRDPDAvLLVLPADhLI-----EDEEAFREavraavEAAEAGKLVTfgikpTR- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 139 eePA------KYGVVVSEPDSGRICRFVEKP-----RVFVSNKI---NAGLYIFSPG-ILQRIQ-LRPTSIE--KEIFPA 200
Cdd:COG0836  148 --PEtgygyiEAGEALGGAGAYKVKRFVEKPdletaEEYLASGNylwNSGMFVFRAStILEELErHAPEIYAalEAAVAA 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 648216203 201 MAQDGQL----------------YA-ME---------LQGFWMDIG 220
Cdd:COG0836  226 AGTDLEVrldaeafaalpsisidYAvMEkadnvavvpADFGWSDVG 271
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 256-351 4.04e-05

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 44.01  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 256 VDPSAKIGANCVIGPNVTIGAGVVVEDGvrikrCTVLQGARIrSHswleSCIVGWSCSVGqwvrmENVTVLGeDVIVNDE 335
Cdd:cd03360   93 VSPSAVIGEGCVIMAGAVINPDARIGDN-----VIINTGAVI-GH----DCVIGDFVHIA-----PGVVLSG-GVTIGEG 156

                         90
                 ....*....|....*..
gi 648216203 336 LYLN-GANVLPHKSIAE 351
Cdd:cd03360  157 AFIGaGATIIQGVTIGA 173
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-225 4.27e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 45.26  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   3 ALILVGGFGTRLRPLTLSRPKPLVEFCNKALL------------LHQLEALRQagvshvvlavsYMSEALEAAMReQEQR 70
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLidipisncinsgINKIYVLTQ-----------FNSASLNRHIS-QTYN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  71 LGiRIS------LSHEKEP------LGTAGP----LALARDllaEGGEPFFVLNSDVICEFPFAALARFHRQHGGEGSIV 134
Cdd:PRK02862  74 FD-GFSggfvevLAAQQTPenpswfQGTADAvrkyLWHFQE---WDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 135 VTRV-EEPAK-YGVVVSEpDSGRICRFVEKPR------------VFVSNKINA---------GLYIFSPGILQRI---QL 188
Cdd:PRK02862 150 VLPVdEKDASgFGLMKTD-DDGRITEFSEKPKgdelkamavdtsRLGLSPEEAkgkpylasmGIYVFSRDVLFDLlnkNP 228

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 648216203 189 RPTSIEKEIFPAMAQDGQLYAMELQGFWMDIGQPKDF 225
Cdd:PRK02862 229 EYTDFGKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAF 265
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 246-315 6.30e-05

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 42.96  E-value: 6.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 246 SGPGVVGNVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVLQGARIRSHSWLESCIVGWSCSVG 315
Cdd:cd05636   28 SGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-320 7.28e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.63  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203   1 MRALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAGVSHVVLAVSYMSEALEAAMREQeqrlgiRISLSHE 80
Cdd:PRK09451   6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADE------PLNWVLQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203  81 KEPLGTAGPLALARDLLAEGgEPFFVLNSDVicefPFAALARFHR-----QHGGEGSIVVTrVEEPAKYGVVVSEpdSGR 155
Cdd:PRK09451  77 AEQLGTGHAMQQAAPFFADD-EDILMLYGDV----PLISVETLQRlrdakPQGGIGLLTVK-LDNPTGYGRITRE--NGK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 156 ICRFVEK----PRVFVSNKINAGLYIFSPGILQR--IQLRPTSIEKEIFP----AMA-QDG-QLYAMelqgfwmdigQPK 223
Cdd:PRK09451 149 VVGIVEQkdatDEQRQIQEINTGILVANGADLKRwlAKLTNNNAQGEYYItdiiALAhQEGrEIVAV----------HPQ 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 224 DF--LTGMCMYLQ------ALRAQHPEKLHsgpgVVGNVLVDPS-------------AKIGANCVIGPNVTIGAGVVVED 282
Cdd:PRK09451 219 RLseVEGVNNRLQlarlerVYQAEQAEKLL----LAGVMLRDPArfdlrgtlthgrdVEIDTNVIIEGNVTLGNRVKIGA 294

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 648216203 283 GVRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRM 320
Cdd:PRK09451 295 GCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFARL 332
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 265-329 1.71e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 40.52  E-value: 1.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648216203 265 NCVIGPNVTIGAGVVVEDGVrikrctVLQGARIRSHSWLESCIVGWSCSVGqwvrmENVTVLGED 329
Cdd:cd04651   28 NSVLFRGVRVGSGSVVEDSV------IMPNVGIGRNAVIRRAIIDKNVVIP-----DGVVIGGDP 81
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 255-329 1.75e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 42.70  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 255 LVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-------------KRCTVLQGARI----------RSHSWLE---SCIV 308
Cdd:PRK12461   7 VIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIgphavilgptrigKNNKIHQGAVVgdepqdftykGEESRLEigdRNVI 86

                         90       100
                 ....*....|....*....|.
gi 648216203 309 GWSCSVGQWVRMENVTVLGED 329
Cdd:PRK12461  87 REGVTIHRGTKGGGVTRIGND 107
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 250-295 1.83e-04

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 42.09  E-value: 1.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 648216203 250 VVGN-VLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-KRCTVlqGA 295
Cdd:cd03360  134 VIGDfVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIgAGAII--GA 179
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 253-332 2.32e-04

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 40.18  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 253 NVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVLQ-----GARIRSHSWLESCIVGWSCSVGQwvrmeNVTVL- 326
Cdd:cd03358   10 NVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTndlypRSKIYRKWELKGTTVKRGASIGA-----NATILp 84

                         90
                 ....*....|
gi 648216203 327 ----GEDVIV 332
Cdd:cd03358   85 gvtiGEYALV 94
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
261-309 2.33e-04

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 40.62  E-value: 2.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648216203 261 KIGANCVIGPNVTIGAG----------------VVVEDGVRI-KRCTVLQGARIRSHswlesCIVG 309
Cdd:COG0110   49 TIGDNVLIGPGVTILTGnhpiddpatfplrtgpVTIGDDVWIgAGATILPGVTIGDG-----AVVG 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 247-309 2.67e-04

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 41.32  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 247 GPGVV--GNVLVDPSAKIGANCVI------------------GPNVTIGAGVVVEDGVRI-KRCTVLQGARIRSHswles 305
Cdd:cd03360  100 GEGCVimAGAVINPDARIGDNVIIntgavighdcvigdfvhiAPGVVLSGGVTIGEGAFIgAGATIIQGVTIGAG----- 174


                 ....
gi 648216203 306 CIVG 309
Cdd:cd03360  175 AIIG 178
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
238-280 2.98e-04

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 40.62  E-value: 2.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 648216203 238 AQHP-EKLHSGPGVVGNVLVDPSAKIGANCVIGPNVTIGAGVVV 280
Cdd:COG0110   65 GNHPiDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVV 108
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 261-314 3.57e-04

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 39.36  E-value: 3.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648216203 261 KIGANCVIGPNVTI-------------------GAGVVVEDGVRI-KRCTVLQGARIRSHswlesCIVGwSCSV 314
Cdd:cd04647   23 TIGDNVLIGPNVTIydhnhdiddperpieqgvtSAPIVIGDDVWIgANVVILPGVTIGDG-----AVVG-AGSV 90
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 241-280 4.09e-04

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 39.36  E-value: 4.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 648216203 241 PEKLHSGPGVVGNvlvdpSAKIGANCVIGPNVTIGAGVVV 280
Cdd:cd04647   51 EQGVTSAPIVIGD-----DVWIGANVVILPGVTIGDGAVV 85
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 262-334 4.19e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 38.71  E-value: 4.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648216203 262 IGANCVIGPNVTI-GA----GVVVEDGVRIKRCtvlqgarirshswlescIVGWSCSVGQWVRMENVTVLGEDVIVND 334
Cdd:cd05787   19 IGRNCKIGKNVVIdNSyiwdDVTIEDGCTIHHS-----------------IVADGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 262-287 4.66e-04

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 39.41  E-value: 4.66e-04
                         10        20
                 ....*....|....*....|....*.
gi 648216203 262 IGANCVIGPNVTIGAGVVVEDGVRIK 287
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQ 26
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
250-276 5.91e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 5.91e-04
                          10        20
                  ....*....|....*....|....*...
gi 648216203  250 VVG-NVLVDPSAKIGANCVIGPNVTIGA 276
Cdd:pfam00132   3 VIGdNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 255-317 1.11e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.01  E-value: 1.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648216203 255 LVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-KRCTVLQGARIRSHSWL-ESCIVGWSCSVGQW 317
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIgDGTWIGPHAVILGPTRIgKNNKIHQGAVVGDE 65
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-54 1.16e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 39.73  E-value: 1.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 648216203   3 ALILVGGFGTRLRPltlSRPKPLVEFCNKALLLHQLEALRQAG-VSHVVLAVS 54
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 245-280 1.47e-03

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 39.40  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 648216203  245 HSGPGVV--GNVLVDPSAKIGANCVIGPNVTIGAGVVV 280
Cdd:TIGR03570 143 HIAPGVTlsGGVVIGEGVFIGAGATIIQGVTIGAGAIV 180
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
253-280 1.69e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|....*...
gi 648216203  253 NVLVDPSAKIGANCVIGPNVTIGAGVVV 280
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 254-283 1.75e-03

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 37.87  E-value: 1.75e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 648216203 254 VLVDPSAKIGANCVIGPNVTIGAGVVVEDG 283
Cdd:cd03358   68 TTVKRGASIGANATILPGVTIGEYALVGAG 97
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 247-286 1.90e-03

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 37.42  E-value: 1.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648216203 247 GPGVV----GNVLVDPSAKIGANCVIGPNVTIGAGV--------VVEDGVRI 286
Cdd:cd03354   12 GPGLFidhgTGIVIGETAVIGDNCTIYQGVTLGGKGkgggkrhpTIGDNVVI 63
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 237-290 3.04e-03

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 37.75  E-value: 3.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648216203 237 RAQHPEKLHSGPGV-VGNVLVDPSAK---------IGANCVIGPNVTIGAGVVVEDGVRIKRCT 290
Cdd:cd03350   49 CAQIGKNVHLSAGAvIGGVLEPLQATpviieddvfIGANCEVVEGVIVGKGAVLAAGVVLTQST 112
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
247-351 3.75e-03

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 37.16  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 247 GPGVV---GNVLVDPSAKIGANCVIGPNVTIGAGvvveDGVRI-KRCTVLQGARIRSHSWlescivGWSCSVGQWVRMEN 322
Cdd:COG0110   12 GDGVVigpGVRIYGGNITIGDNVYIGPGVTIDDP----GGITIgDNVLIGPGVTILTGNH------PIDDPATFPLRTGP 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 648216203 323 VTVlGEDVIVndelylnGAN--VLPHKSIAE 351
Cdd:COG0110   82 VTI-GDDVWI-------GAGatILPGVTIGD 104
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-54 4.28e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 38.19  E-value: 4.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648216203   4 LILVGGFGTRLRpltLSRPKPLVEFCNKALLLHQLEALRQAG-VSHVVLAVS 54
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 248-354 4.94e-03

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 37.35  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648216203 248 PGVVGNVLVDPSAKIGANCVIGPNVTIGAG---------VVVEDGVRIKRCTVLQG-----------ARIRSHSWLESCI 307
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHaslrgdfgrIVIRDGANVQDNCVIHGfpgqdtvleenGHIGHGAILHGCT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 648216203 308 VGWSCSVG-QWVRMENVTVlGEDVIVNDELYLNGANVLPHKSIAESVP 354
Cdd:cd04745   81 IGRNALVGmNAVVMDGAVI-GEESIVGAMAFVKAGTVIPPRSLIAGSP 127
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 254-332 5.05e-03

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 35.69  E-value: 5.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648216203 254 VLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRIKRCTVLQGARIrshswlesCIVGWSCSVGQWVRMENVTVLGEDVIV 332
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNP--------TIIGDNVEIGANAVIHGGVKIGDNAVI 71
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 250-286 5.38e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.77  E-value: 5.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 648216203 250 VVGNVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI 286
Cdd:cd03352  141 IAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVI 177
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 260-334 8.85e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 35.52  E-value: 8.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648216203 260 AKIGANCVIgPNVTIGAGVVVEDGvRIKRCTVLQGARIRSHSWLESCIVGWSCSVGQWVRMENVtVLGEDVIVND 334
Cdd:cd04651    2 PYIGRRGEV-KNSLVSEGCIISGG-TVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRA-IIDKNVVIPD 73
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
253-300 9.19e-03

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.39  E-value: 9.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 648216203 253 NVLVDPSAKIGANCVIGPNVTIGAGVVVEDGVRI-KRCTVLQGARIRSH 300
Cdd:PRK05289   2 MAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIgDGTVIGSHVVIDGH 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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