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Conserved domains on  [gi|1056649767|ref|WP_068078258|]
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DegT/DnrJ/EryC1/StrS aminotransferase family protein [Novosphingobium lentum]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10001360)

DegT/DnrJ/EryC1/StrS family aminotransferase such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

CATH:  3.40.640.10|3.90.1150.10
EC:  2.6.1.-
Gene Ontology:  GO:0008483
PubMed:  17109392
SCOP:  4000675

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
21-405 8.34e-144

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 413.31  E-value: 8.34e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  21 WPRHDDDEIDAVVKVLRSGRvnaLVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFA 100
Cdd:COG0399     6 RPSIGEEEIAAVVEVLRSGW---LTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 101 TASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRG 180
Cdd:COG0399    83 TANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 181 QPVGSFGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHGKDPYKmrtpvpslpgqfRFLHDSFGTNFRITEL 260
Cdd:COG0399   163 KKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA------------KYEHVELGYNYRMDEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 261 QAAIGRVQLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNPAWYKFYARydsisIPGAPSRDALIAAMLARGIA 340
Cdd:COG0399   230 QAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIR-----LDEGEDRDELIAALKARGIG 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056649767 341 CGSGSCPDMSRENAFAQYPPRRdGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEqvemAFRDCL 405
Cdd:COG0399   305 TRVHYPIPLHLQPAYRDLGYRP-GDLPVAERLAERVLSLPLHPGLTEEDVDRVIE----AIREFL 364
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
21-405 8.34e-144

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 413.31  E-value: 8.34e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  21 WPRHDDDEIDAVVKVLRSGRvnaLVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFA 100
Cdd:COG0399     6 RPSIGEEEIAAVVEVLRSGW---LTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 101 TASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRG 180
Cdd:COG0399    83 TANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 181 QPVGSFGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHGKDPYKmrtpvpslpgqfRFLHDSFGTNFRITEL 260
Cdd:COG0399   163 KKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA------------KYEHVELGYNYRMDEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 261 QAAIGRVQLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNPAWYKFYARydsisIPGAPSRDALIAAMLARGIA 340
Cdd:COG0399   230 QAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIR-----LDEGEDRDELIAALKARGIG 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056649767 341 CGSGSCPDMSRENAFAQYPPRRdGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEqvemAFRDCL 405
Cdd:COG0399   305 TRVHYPIPLHLQPAYRDLGYRP-GDLPVAERLAERVLSLPLHPGLTEEDVDRVIE----AIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 28-398 6.79e-137

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 395.37  E-value: 6.79e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  28 EIDAVVKVLRSGRVNalvHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFATASSVAA 107
Cdd:cd00616     1 ELEAVEEVLDSGWLT---LGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 108 VGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRGQPVGSFG 187
Cdd:cd00616    78 LGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 188 DASSFSFCTDKIMsTGGEGGMVLFRQEEAWARAFAYKDHGKDPYKmrtpvpslpgqFRFLHDSFGTNFRITELQAAIGRV 267
Cdd:cd00616   158 DAGAFSFHPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDR-----------FKYEHEILGYNYRLSEIQAAIGLA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 268 QLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNPAWYKFYARYDSisiPGAPSRDALIAAMLARGIACGsGSCP 347
Cdd:cd00616   226 QLEKLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDP---EAGESRDELIEALKEAGIETR-VHYP 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1056649767 348 DMSRENAFAQYPPRRDGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEQVE 398
Cdd:cd00616   302 PLHHQPPYKKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 22-398 7.53e-115

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 339.64  E-value: 7.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  22 PRHDDDEIDAVVKVLRSGRvnaLVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFAT 101
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGW---LTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 102 ASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRGQ 181
Cdd:pfam01041  78 ANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 182 PVGSFGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHGKDPYKMRtpvpslpgqfRFLHDSFGTNFRITELQ 261
Cdd:pfam01041 158 KVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKADK----------RYWHEVLGYNYRMTEIQ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 262 AAIGRVQLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNP-AWYKFyarydSISIP-GAPSRDALIAAMLARGI 339
Cdd:pfam01041 227 AAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVhAWHLF-----PILVPeEAINRDELVEALKEAGI 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1056649767 340 ACGSGSCPDMSRENAFAQYPPRRDGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEQVE 398
Cdd:pfam01041 302 GTRVHYPIPLHLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 25-292 2.49e-72

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 231.06  E-value: 2.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  25 DDDEIDAVVKVLRSgrvNALVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFATASS 104
Cdd:TIGR03588   9 DQDDIDAVVEVLKS---DFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 105 VAAVGADPVFADIVQETQNIDPASIARMI----GPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRG 180
Cdd:TIGR03588  86 ALYCGAKVDFVDIDPDTGNIDEDALEKKLaaakGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 181 QPVGS--FGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHG--KDPYKMRTPVpslPGQFRFLHDSFGTNFR 256
Cdd:TIGR03588 166 KPVGNcrYADATVFSFHPVKIITT-AEGGAVTTNDEELAERMRLLRSHGitKDPLLFEKQD---EGPWYYEQQELGFNYR 241

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1056649767 257 ITELQAAIGRVQLAKLPGWLDRRRQNAATLASALEG 292
Cdd:TIGR03588 242 MTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKD 277
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
22-342 3.42e-56

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 189.08  E-value: 3.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  22 PRHDDDEIDAVVKVLRSGRVNAlvhGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFAT 101
Cdd:PRK11658   10 PAMGDEELAAVKEVLRSGWITT---GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVST 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 102 ASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRGQ 181
Cdd:PRK11658   87 LNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 182 PVGSFGDAsSFSFCTDKIMsTGGEGGMVLFRQEEAWARAFAYKDHG--KDPYKM----RTPvpslpgQFRFLHDSFGTNf 255
Cdd:PRK11658  167 HIGARGTA-IFSFHAIKNI-TCAEGGLVVTDDDELADRLRSLKFHGlgVDAFDRqtqgRAP------QAEVLTPGYKYN- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 256 rITELQAAIGRVQLAKLPGWLDRRRQNAATLASALEGVRgmiVDPVPVDVNP---AWYKFYARYDSISIpgAPSRDALIA 332
Cdd:PRK11658  238 -LADINAAIALVQLAKLEALNARRREIAARYLQALADLP---FQPLSLPAWPhqhAWHLFIIRVDEERC--GISRDALME 311

                         330
                  ....*....|
gi 1056649767 333 AMLARGIACG 342
Cdd:PRK11658  312 ALKERGIGTG 321
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
21-405 8.34e-144

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 413.31  E-value: 8.34e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  21 WPRHDDDEIDAVVKVLRSGRvnaLVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFA 100
Cdd:COG0399     6 RPSIGEEEIAAVVEVLRSGW---LTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 101 TASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRG 180
Cdd:COG0399    83 TANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 181 QPVGSFGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHGKDPYKmrtpvpslpgqfRFLHDSFGTNFRITEL 260
Cdd:COG0399   163 KKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA------------KYEHVELGYNYRMDEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 261 QAAIGRVQLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNPAWYKFYARydsisIPGAPSRDALIAAMLARGIA 340
Cdd:COG0399   230 QAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIR-----LDEGEDRDELIAALKARGIG 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056649767 341 CGSGSCPDMSRENAFAQYPPRRdGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEqvemAFRDCL 405
Cdd:COG0399   305 TRVHYPIPLHLQPAYRDLGYRP-GDLPVAERLAERVLSLPLHPGLTEEDVDRVIE----AIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 28-398 6.79e-137

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 395.37  E-value: 6.79e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  28 EIDAVVKVLRSGRVNalvHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFATASSVAA 107
Cdd:cd00616     1 ELEAVEEVLDSGWLT---LGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 108 VGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRGQPVGSFG 187
Cdd:cd00616    78 LGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 188 DASSFSFCTDKIMsTGGEGGMVLFRQEEAWARAFAYKDHGKDPYKmrtpvpslpgqFRFLHDSFGTNFRITELQAAIGRV 267
Cdd:cd00616   158 DAGAFSFHPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDR-----------FKYEHEILGYNYRLSEIQAAIGLA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 268 QLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNPAWYKFYARYDSisiPGAPSRDALIAAMLARGIACGsGSCP 347
Cdd:cd00616   226 QLEKLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDP---EAGESRDELIEALKEAGIETR-VHYP 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1056649767 348 DMSRENAFAQYPPRRDGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEQVE 398
Cdd:cd00616   302 PLHHQPPYKKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 22-398 7.53e-115

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 339.64  E-value: 7.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  22 PRHDDDEIDAVVKVLRSGRvnaLVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFAT 101
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGW---LTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 102 ASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRGQ 181
Cdd:pfam01041  78 ANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 182 PVGSFGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHGKDPYKMRtpvpslpgqfRFLHDSFGTNFRITELQ 261
Cdd:pfam01041 158 KVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKADK----------RYWHEVLGYNYRMTEIQ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 262 AAIGRVQLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPVDVNP-AWYKFyarydSISIP-GAPSRDALIAAMLARGI 339
Cdd:pfam01041 227 AAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVhAWHLF-----PILVPeEAINRDELVEALKEAGI 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1056649767 340 ACGSGSCPDMSRENAFAQYPPRRDGDLPEARRLGQTSLMFAVDHLFEPADMEHVGEQVE 398
Cdd:pfam01041 302 GTRVHYPIPLHLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 25-292 2.49e-72

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 231.06  E-value: 2.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  25 DDDEIDAVVKVLRSgrvNALVHGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFATASS 104
Cdd:TIGR03588   9 DQDDIDAVVEVLKS---DFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 105 VAAVGADPVFADIVQETQNIDPASIARMI----GPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRG 180
Cdd:TIGR03588  86 ALYCGAKVDFVDIDPDTGNIDEDALEKKLaaakGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 181 QPVGS--FGDASSFSFCTDKIMSTgGEGGMVLFRQEEAWARAFAYKDHG--KDPYKMRTPVpslPGQFRFLHDSFGTNFR 256
Cdd:TIGR03588 166 KPVGNcrYADATVFSFHPVKIITT-AEGGAVTTNDEELAERMRLLRSHGitKDPLLFEKQD---EGPWYYEQQELGFNYR 241

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1056649767 257 ITELQAAIGRVQLAKLPGWLDRRRQNAATLASALEG 292
Cdd:TIGR03588 242 MTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKD 277
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
22-342 3.42e-56

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 189.08  E-value: 3.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  22 PRHDDDEIDAVVKVLRSGRVNAlvhGDQCRSFEQEFADFTTMPFAIAVANGTVSLELALRALGVRHGDEVIVPARSFFAT 101
Cdd:PRK11658   10 PAMGDEELAAVKEVLRSGWITT---GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVST 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 102 ASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGALYRGQ 181
Cdd:PRK11658   87 LNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 182 PVGSFGDAsSFSFCTDKIMsTGGEGGMVLFRQEEAWARAFAYKDHG--KDPYKM----RTPvpslpgQFRFLHDSFGTNf 255
Cdd:PRK11658  167 HIGARGTA-IFSFHAIKNI-TCAEGGLVVTDDDELADRLRSLKFHGlgVDAFDRqtqgRAP------QAEVLTPGYKYN- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 256 rITELQAAIGRVQLAKLPGWLDRRRQNAATLASALEGVRgmiVDPVPVDVNP---AWYKFYARYDSISIpgAPSRDALIA 332
Cdd:PRK11658  238 -LADINAAIALVQLAKLEALNARRREIAARYLQALADLP---FQPLSLPAWPhqhAWHLFIIRVDEERC--GISRDALME 311

                         330
                  ....*....|
gi 1056649767 333 AMLARGIACG 342
Cdd:PRK11658  312 ALKERGIGTG 321
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 25-339 4.03e-50

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 174.69  E-value: 4.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  25 DDDEIDAVVKV-----LRSGRVNAlvhgdqcrSFEQEFADFTTMPFAIAVANGT----------VSLELALRALgvRHGD 89
Cdd:PRK15407   43 DAKELQNLVDAsldfwLTTGRFND--------AFEKKLAEFLGVRYALLVNSGSsanllafsalTSPKLGDRAL--KPGD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  90 EVIVPARSFFATASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIED 169
Cdd:PRK15407  113 EVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIED 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 170 CAQAHGALYRGQPVGSFGDASSFSFCTDKIMsTGGEGGMVLFRQEEAWARAFAYKDHGKDPYkmrtpvpSLPG------- 242
Cdd:PRK15407  193 NCDALGSTYDGRMTGTFGDIATLSFYPAHHI-TMGEGGAVFTNDPLLKKIIESFRDWGRDCW-------CAPGcdntcgk 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 243 ----QF---------RFLHDSFGTNFRITELQAAIGRVQLAKLPGWLDRRRQNAATLASALEGVRGMIVDPVPV-DVNPA 308
Cdd:PRK15407  265 rfgwQLgelpfgydhKYTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDFLILPEATpNSDPS 344

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1056649767 309 WYKFyarydSISI-PGAP-SRDALIAAMLARGI 339
Cdd:PRK15407  345 WFGF-----PITVkEDAGfTRVELVKYLEENKI 372
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 28-339 1.49e-45

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 161.16  E-value: 1.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  28 EIDAVVKVLRSGRVnalvHGD-----QC-RSFEQEF----ADFTTmpfaiavaNGTVSLELALRALGVRHGDEVIVPARS 97
Cdd:PRK11706   13 ELDYIQQAMSSGKL----CGDggftrRCqQWLEQRFgsakVLLTP--------SCTAALEMAALLLDIQPGDEVIMPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  98 FFATASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVICVHLAGRPCDMGPIVNLCREQGLVLIEDCAQAHGAL 177
Cdd:PRK11706   81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 178 YRGQPVGSFGDASSFSFCTDKIMsTGGEGGMVLFRQEEAWARAFAYKDHGKDpykmRTPVpslpgqFRFLHDSF-----G 252
Cdd:PRK11706  161 YKGRALGTIGHIGCFSFHETKNY-TAGEGGALLINDPALIERAEIIREKGTN----RSQF------FRGQVDKYtwvdiG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 253 TNFRITELQAAIGRVQLAKLPGWLDRRR---QN-AATLASALEgvRGMIVDP-VPVDVNPAWYKFYarydsISIPGAPSR 327
Cdd:PRK11706  230 SSYLPSELQAAYLWAQLEAADRINQRRLalwQRyYDALAPLAE--AGRIELPsIPDDCKHNAHMFY-----IKLRDLEDR 302

                         330
                  ....*....|..
gi 1056649767 328 DALIAAMLARGI 339
Cdd:PRK11706  303 SALINFLKEAGI 314
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 67-169 1.65e-09

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 58.99  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  67 IAVANG-TVSLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQ-NIDPASIARMIGPRTRAVI--- 141
Cdd:COG0436    93 ILVTNGaKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENGfLPDPEALEAAITPRTKAIVlns 171

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1056649767 142 -------CVHLAgrpcDMGPIVNLCREQGLVLIED 169
Cdd:COG0436   172 pnnptgaVYSRE----ELEALAELAREHDLLVISD 202
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 67-355 1.77e-07

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 52.73  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  67 IAVANGTV-SLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQE-TQNIDPASIARMIGPRTRAVICVH 144
Cdd:cd00609    62 IVVTNGAQeALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLYLNN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 145 L---AGRpcDMGP-----IVNLCREQGLVLIEDcaQAHGALYRGQPVGSFGDA----------SSFSfctdKIMSTGGE- 205
Cdd:cd00609   141 PnnpTGA--VLSEeeleeLAELAKKHGILIISD--EAYAELVYDGEPPPALALldayervivlRSFS----KTFGLPGLr 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 206 GGMVLFRQEEAWARAFAYKDhgkdpykMRTPVPSLPGQF---RFLHDsfgtnfritelqaaiGRVQLAKLPGWLDRRRQn 282
Cdd:cd00609   213 IGYLIAPPEELLERLKKLLP-------YTTSGPSTLSQAaaaAALDD---------------GEEHLEELRERYRRRRD- 269

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1056649767 283 aaTLASALEGVRGMIVdPVPVDVNPAWykfyarydsISIPGAPSRDALIAAMLARGIACGSGSCPDMSRENAF 355
Cdd:cd00609   270 --ALLEALKELGPLVV-VKPSGGFFLW---------LDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFV 330
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 53-212 1.26e-06

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 48.15  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  53 FEQEFADFTT--MPFAIAVANGTVSLELALRALgVRHGDEVIVPARSFFA-TASSVAAVGADPVFADIVQETQNIDPASI 129
Cdd:cd01494     5 LEEKLARLLQpgNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGGLDVAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767 130 A--RMIGPRTRAVICVHLAGRPCDMGPIVN---LCREQGLVLIEDCAQAHGALYRGQPVGSFGDASSFSFCTDKIMsTGG 204
Cdd:cd01494    84 LeeLKAKPNVALIVITPNTTSGGVLVPLKEirkIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNL-GGE 162


                  ....*...
gi 1056649767 205 EGGMVLFR 212
Cdd:cd01494   163 GGGVVIVK 170
PRK07682 PRK07682
aminotransferase;
75-141 2.06e-06

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 49.35  E-value: 2.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1056649767  75 SLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQ-NIDPASIARMIGPRTRAVI 141
Cdd:PRK07682   93 ALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENEfKVQPAQIEAAITAKTKAIL 159
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 67-141 9.24e-06

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 47.43  E-value: 9.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056649767  67 IAVANGT-VSLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQ-NIDPASIARMIGPRTRAVI 141
Cdd:PRK05764   94 VIVTTGAkQALYNAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENGfKLTVEQLEAAITPKTKALI 169
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
67-173 1.08e-04

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 43.97  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  67 IAVANGTVSLELALRALG-VRHGDEV----------IVPARSffatasSVAAVGADPVFADIvQETQNIDPASIARMIGP 135
Cdd:COG0520    81 IFTRGTTEAINLVAYGLGrLKPGDEIlitemehhsnIVPWQE------LAERTGAEVRVIPL-DEDGELDLEALEALLTP 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1056649767 136 RTRAVICVHLA---GRPCDMGPIVNLCREQG-LVLIeDCAQA 173
Cdd:COG0520   154 RTKLVAVTHVSnvtGTVNPVKEIAALAHAHGaLVLV-DGAQS 194
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 66-179 1.16e-04

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 43.93  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  66 AIAVANGTVSLELALRALgVRHGDEVIVpARSFFAT-----ASSVAAVGADPVFADivqetqNIDPASIARMIGPRTRAV 140
Cdd:PRK05994   81 ALAVASGHAAQFLVFHTL-LQPGDEFIA-ARKLYGGsinqfGHAFKSFGWQVRWAD------ADDPASFERAITPRTKAI 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1056649767 141 ICVHLA---GRPCDMGPIVNLCREQGLVLIEDCAQAHGALYR 179
Cdd:PRK05994  153 FIESIAnpgGTVTDIAAIAEVAHRAGLPLIVDNTLASPYLIR 194
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
78-141 1.60e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 43.56  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056649767  78 LALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQ-NIDPASIARMIGPRTRAVI 141
Cdd:PRK06348  104 LALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILETYEEDGfQINVKKLEALITSKTKAII 167
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 67-173 2.99e-04

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 42.45  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  67 IAVANGTVSLELALRALGVRH--GDEVIVparSFFATASSV-------AAVGADPVFADiVQETQNIDPASIARMIGPRT 137
Cdd:cd06453    65 IFTRNTTEAINLVAYGLGRANkpGDEIVT---SVMEHHSNIvpwqqlaERTGAKLKVVP-VDDDGQLDLEALEKLLTERT 140

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1056649767 138 RAVICVHLA---GRPCDMGPIVNLCREQGLVLIEDCAQA 173
Cdd:cd06453   141 KLVAVTHVSnvlGTINPVKEIGEIAHEAGVPVLVDGAQS 179
PRK08363 PRK08363
alanine aminotransferase; Validated
 64-169 3.25e-03

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 39.41  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  64 PFAIAVANG-TVSLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQ-NIDPASIARMIGPRTRAvI 141
Cdd:PRK08363   93 PDDVRVTAAvTEALQLIFGAL-LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRTIEEEGwQPDIDDIRKKITEKTKA-I 170

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1056649767 142 CVHLAGRPC-------DMGPIVNLCREQGLVLIED 169
Cdd:PRK08363  171 AVINPNNPTgalyekkTLKEILDIAGEHDLPVISD 205
PRK09082 PRK09082
methionine aminotransferase; Validated
 70-141 3.58e-03

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 39.13  E-value: 3.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056649767  70 ANGTVSLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVI 141
Cdd:PRK09082   98 AGATEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLII 168
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
75-141 3.87e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 39.02  E-value: 3.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056649767  75 SLELALRALgVRHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQNIDPASIARMIGPRTRAVI 141
Cdd:PRK06836  108 ALNVALKAI-LNPGDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVI 173
PRK07550 PRK07550
aminotransferase;
86-169 4.77e-03

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 38.79  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056649767  86 RHGDEVIVPARSFFATASSVAAVGADPVFADIVQETQNI-DPASIARMIGPRTRAVICVHlAGRPCD-------MGPIVN 157
Cdd:PRK07550  112 GAGDEVILPLPWYFNHKMWLDMLGIRPVYLPCDEGPGLLpDPAAAEALITPRTRAIALVT-PNNPTGvvyppelLHELYD 190

                          90
                  ....*....|..
gi 1056649767 158 LCREQGLVLIED 169
Cdd:PRK07550  191 LARRHGIALILD 202
 
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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