NCBI Conserved Domain Search

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...

107-312

1.48e-103

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: 302.41 E-value: 1.48e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 107 SAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNARD 186
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 187 EdGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQIAHNVVIGRNTALAGVTAVAGSTTIGDNCLI 266
Cdd:cd03352   81 G-GGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVII 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489115220 267 GGQSAITGHISICDNTIIGGASNIGkSITKPGMYYAAFEAKPRIQW 312
Cdd:cd03352  160 GGQVGIAGHLTIGDGVVIGAGSGVT-SIVPPGEYVSGTPAQPHREW 204

LpxD

pfam04613

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...

21-87

2.01e-20

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins.

Pssm-ID: 461366 [Multi-domain] Cd Length: 69 Bit Score: 83.70 E-value: 2.01e-20

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115220   21 VEIKKIATLSLAGEGDISFCTNPKYLKALSETKASAVLITEEVLEFCNTNAVVL--SNPYMALAKVMEL 87
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATATLLvvDNPYLAFAKLLQL 69

Name

Accession

Description

Interval

E-value

LpxD

COG1044

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...

1-335

8.99e-167

Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 467.57 E-value: 8.99e-167

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220   1 MYSLDFLASKLDGEVKGDKNVEIKKIATLSLAGEGDISFCTNPKYLKALSETKASAVLITEEVLEFC-NTNAVVLSNPYM 79
Cdd:COG1044    1 SFTLAELAELLGGELVGDGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALpGLALIVVDNPYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  80 ALAKVMELFDKSPRPDGKIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIA 159
Cdd:COG1044   81 AFAKLLQLFYPPPAPAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 160 HDVVIGTGCIIHQNAVIGCDGFGNARDEDGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQIAHN 239
Cdd:COG1044  161 ERCVIGDRVIIHSGAVIGADGFGFAPDEDGGWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 240 VVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMyYAAFEAKPRIQWGRFVAKL 319
Cdd:COG1044  241 VRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGV-YSGSPAQPHREWLRNAAAL 319

                        330
                 ....*....|....*.
gi 489115220 320 AKIDTLITKVKQLEEK 335
Cdd:COG1044  320 RRLPELAKRLKELEKK 335

lpxD

PRK00892

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

1-337

2.33e-165

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

Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 464.23 E-value: 2.33e-165

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220   1 MYSLDFLASKLDGEVKGDKNVEIKKIATLSLAGEGDISFCTNPKYLKALSETKASAVLITEEVLEFC--NTNAVVLSNPY 78
Cdd:PRK00892   2 SLTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVpaGNALLVVKNPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  79 MALAKVMELFDKSPRPDGK--IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNV 156
Cdd:PRK00892  82 LAFARLAQLFDPPATPSPAagIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 157 SIAHDVVIGTGCIIHQNAVIGCDGFGNArDEDGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQI 236
Cdd:PRK00892 162 TIYHAVRIGNRVIIHSGAVIGSDGFGFA-NDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 237 AHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMYYAAFEAKPRIQWGRFV 316
Cdd:PRK00892 241 AHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTA 320

                        330       340
                 ....*....|....*....|.
gi 489115220 317 AKLAKIDTLITKVKQLEEKIK 337
Cdd:PRK00892 321 ARLRRLDELRKRLKALEKKVE 341

lipid_A_lpxD

TIGR01853

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...

7-329

3.33e-123

Pssm-ID: 273834 [Multi-domain] Cd Length: 324 Bit Score: 356.60 E-value: 3.33e-123

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220    7 LASKLDGEVKGDKNVEIKKIATLSLAGEGDISFCTNPKYLKALSETKASAVLITEE-VLEFCNTNAVVLSNPYMALAKVM 85
Cdd:TIGR01853   2 LAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDdQGLPAKCAALVVKDPYLAFAKVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220   86 ELFDKSPRPDGKIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIG 165
Cdd:TIGR01853  82 ELFDPPPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQLG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  166 TGCIIHQNAVIGCDGFGNARDEDGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQIAHNVVIGRN 245
Cdd:TIGR01853 162 KNVIIHSGAVIGSDGFGYAHTANGGHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIGEN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  246 TALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMyYAAFEAKPRIQWGRFVAKLAKIDTL 325
Cdd:TIGR01853 242 CIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGV-YGGIPARPNKEWLRIAAKVKRLPEL 320


                  ....
gi 489115220  326 ITKV 329
Cdd:TIGR01853 321 RKRI 324

LbH_LpxD

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...

107-312

1.48e-103

Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 302.41 E-value: 1.48e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 107 SAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNARD 186
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 187 EdGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQIAHNVVIGRNTALAGVTAVAGSTTIGDNCLI 266
Cdd:cd03352   81 G-GGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVII 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489115220 267 GGQSAITGHISICDNTIIGGASNIGkSITKPGMYYAAFEAKPRIQW 312
Cdd:cd03352  160 GGQVGIAGHLTIGDGVVIGAGSGVT-SIVPPGEYVSGTPAQPHREW 204

LpxA

COG1043

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...

97-292

2.15e-32

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: 121.28 E-value: 2.15e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDtliksnvsiahdvvigtgCIIHQNAVI 176
Cdd:COG1043    3 MIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKN------------------NRIFPFASI 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 177 GCDgfgnardedgswtkiPQ-LG------RVIIEDDVEIGSGTTVDRGAIDD---TIIkkGAriDNL----VQIAHNVVI 242
Cdd:COG1043   65 GEE---------------PQdLKykgeptRLEIGDNNTIREFVTIHRGTVQGggvTRI--GD--DNLlmayVHVAHDCVV 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489115220 243 GRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGK 292
Cdd:COG1043  126 GNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVK 175

LbH_UDP-GlcNAc_AT

cd03351

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...

97-292

1.70e-30

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: 115.99 E-value: 1.70e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDtliksnvsiahdvvigtgCIIHQNAVI 176
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKN------------------NRIFPFASI 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 177 GCDgfgnardedgswtkiPQ-LG------RVIIEDDVEIGSGTTVDRGAIDD---TIIkkGAriDNL----VQIAHNVVI 242
Cdd:cd03351   63 GEA---------------PQdLKykgeptRLEIGDNNTIREFVTIHRGTAQGggvTRI--GN--NNLlmayVHVAHDCVI 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489115220 243 GRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGK 292
Cdd:cd03351  124 GNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQ 173

PRK05289

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

97-292

2.15e-28

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

Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 110.57 E-value: 2.15e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDtliksnvsiahdvvigtgCIIHQNAVI 176
Cdd:PRK05289   4 KIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKN------------------NRIFPFASI 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 177 GCDgfgnardedgswtkiPQ-LG------RVIIEDDVEIGSGTTVDRGAIDD---TIIkkGAriDNL----VQIAHNVVI 242
Cdd:PRK05289  66 GED---------------PQdLKykgeptRLVIGDNNTIREFVTINRGTVQGggvTRI--GD--NNLlmayVHVAHDCVV 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489115220 243 GRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGK 292
Cdd:PRK05289 127 GNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQ 176

lipid_A_lpxA

TIGR01852

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...

98-294

2.17e-25

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

Pssm-ID: 188173 [Multi-domain] Cd Length: 254 Bit Score: 102.34 E-value: 2.17e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220   98 IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNdtliksnvsiahdvvigtGCIIHQNAVIG 177
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGE------------------GTRIFPGAVIG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  178 CDgfgnarDEDGSWTkiPQLGRVIIEDDVEIGSGTTVDRG-AIDDTIIKKGAriDNL----VQIAHNVVIGRNTALAGVT 252
Cdd:TIGR01852  63 GV------PQDLKYK--GEKTRLIIGDNNTIREFVTINRGtASGGGVTRIGN--NNLlmaySHIAHDCVVGNHVILANNA 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 489115220  253 AVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSI 294
Cdd:TIGR01852 133 TLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDV 174

PRK12461

UDP-N-acetylglucosamine acyltransferase; Provisional

98-292

2.02e-24

UDP-N-acetylglucosamine acyltransferase; Provisional

Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 99.71 E-value: 2.02e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  98 IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDtliksnvsiahdvvigtgCIIHQNAVIG 177
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKN------------------NKIHQGAVVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 178 CDgfgnarDEDGSWTKIPQlgRVIIEDDVEIGSGTTVDRGAIDDTIIKKGAriDNL----VQIAHNVVIGRNTALAGVTA 253
Cdd:PRK12461  64 DE------PQDFTYKGEES--RLEIGDRNVIREGVTIHRGTKGGGVTRIGN--DNLlmaySHVAHDCQIGNNVILVNGAL 133

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489115220 254 VAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGK 292
Cdd:PRK12461 134 LAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISK 172

LpxD

pfam04613

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...

21-87

2.01e-20

Pssm-ID: 461366 [Multi-domain] Cd Length: 69 Bit Score: 83.70 E-value: 2.01e-20

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115220   21 VEIKKIATLSLAGEGDISFCTNPKYLKALSETKASAVLITEEVLEFCNTNAVVL--SNPYMALAKVMEL 87
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATATLLvvDNPYLAFAKLLQL 69

LbH_AT_putative

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...

98-216

6.96e-17

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: 77.52 E-value: 6.96e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  98 IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIg 177
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATI- 165

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115220 178 cdgfgnardedgswtkipqLGRVIIEDDVEIGSGTTVDR 216
Cdd:cd03360  166 -------------------IQGVTIGAGAIIGAGAVVTK 185

NeuD_NnaD

TIGR03570

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...

98-214

1.67e-15

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: 74.07 E-value: 1.67e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220   98 IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIg 177
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATI- 168

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489115220  178 cdgfgnardedgswtkipqLGRVIIEDDVEIGSGTTV 214
Cdd:TIGR03570 169 -------------------IQGVTIGAGAIVGAGAVV 186

LbH_AT_putative

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...

150-301

9.94e-13

Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 65.97 E-value: 9.94e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 150 TLIKSNVSIAHDVVIGTGCIIHQNAVIGCDgfgnardedgswtkipqlgrviieddVEIGSGTTVDRGAIddtiikkgar 229
Cdd:cd03360   85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPD--------------------------ARIGDNVIINTGAV---------- 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115220 230 idnlvqIAHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMYY 301
Cdd:cd03360  129 ------IGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVV 194

WbbJ

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

108-286

1.58e-12

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

Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 64.12 E-value: 1.58e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 108 AIIGENVTIGANAVV-GENVVIGDNVYIGACATIDNGtkigndtliksnvsiaHDVVIGTGCIIHQNAVIgCDGFGNARD 186
Cdd:COG0110    9 ARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDP----------------GGITIGDNVLIGPGVTI-LTGNHPIDD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 187 EDGSWTKIpqlGRVIIEDDVEIGSGTTVdrgaiddtiikkgaridnlvqiahnvvigrntaLAGVtavagstTIGDNCLI 266
Cdd:COG0110   72 PATFPLRT---GPVTIGDDVWIGAGATI---------------------------------LPGV-------TIGDGAVV 108

                        170       180
                 ....*....|....*....|
gi 489115220 267 GGQSAITGHISicDNTIIGG 286
Cdd:COG0110  109 GAGSVVTKDVP--PYAIVAG 126

LbH_AT_putative

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...

103-230

3.13e-12

Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 64.43 E-value: 3.13e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 103 VIAASAIIGENVTIGANAVVGENVVIGdnvyigacatidNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGcdgfg 182
Cdd:cd03360   86 LIHPSAVVSPSAVIGEGCVIMAGAVIN------------PDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLS----- 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489115220 183 nardedgswtkipqlGRVIIEDDVEIGSGTTVdrgaIDDTIIKKGARI 230
Cdd:cd03360  149 ---------------GGVTIGEGAFIGAGATI----IQGVTIGAGAII 177

PaaY

COG0663

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...

86-214

4.75e-11

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];

Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 60.43 E-value: 4.75e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  86 ELFDKSPRpdgkIHSKAVIAASA-IIGeNVTIGANAVVGENVVI-GDN--VYIGACATIDNGTKI----GNDTLIKSNVS 157
Cdd:COG0663    5 SFDGKTPQ----IHPSAFVAPTAvVIG-DVTIGEDVSVWPGAVLrGDVgpIRIGEGSNIQDGVVLhvdpGYPLTIGDDVT 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115220 158 IAHDVVIgTGCIIHQNAVIG-----CDGfgnardedgswtkipqlgrVIIEDDVEIGSGTTV 214
Cdd:COG0663   80 IGHGAIL-HGCTIGDNVLIGmgaivLDG-------------------AVIGDGSIVGAGALV 121

LbH_gamma_CA_like

cd04645

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...

97-230

2.48e-10

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.

Pssm-ID: 100051 [Multi-domain] Cd Length: 153 Bit Score: 58.19 E-value: 2.48e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASA-IIGeNVTIGANAVVGENVVI-GDN--VYIGACATIDNGTKI----GNDTLIKSNVSIAHDVVIgTGC 168
Cdd:cd04645    1 EIDPSAFIAPNAtVIG-DVTLGEGSSVWFGAVLrGDVnpIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVL-HGC 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115220 169 IIHQNAVIGcdgfgnardeDGSwtkipqlgrvIIEDDVEIGSGTTVDRGAiddtIIKKGARI 230
Cdd:cd04645   79 TIGDNCLIG----------MGA----------IILDGAVIGKGSIVAAGS----LVPPGKVI 116

LbH_WxcM_N_like

cd03358

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...

128-214

4.31e-10

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: 56.74 E-value: 4.31e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 128 IGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNARDEDGSWtkipqLGRVIIEDDVE 207
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWE-----LKGTTVKRGAS 75


                 ....*..
gi 489115220 208 IGSGTTV 214
Cdd:cd03358   76 IGANATI 82

GlmU

COG1207

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...

104-273

5.22e-10

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: 60.04 E-value: 5.22e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 104 IAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNgTKIGNDTLIKSnvSIAHDVVIGTGCII------------H 171
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD-STIGDGVVIKY--SVIEDAVVGAGATVgpfarlrpgtvlG 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 172 QNAVIGcdGFG---NARDEDGSwtKIPQL---GRVIIEDDVEIGSGT-TV--D-----RgaiddTIIKKGARidnlvqia 237
Cdd:COG1207  340 EGVKIG--NFVevkNSTIGEGS--KVNHLsyiGDAEIGEGVNIGAGTiTCnyDgvnkhR-----TVIGDGAF-------- 402

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489115220 238 hnvvIGRNTAL-AGVtavagstTIGDNCLIGGQSAIT 273
Cdd:COG1207  403 ----IGSNTNLvAPV-------TIGDGATIGAGSTIT 428

LbH_GlmU_C

cd03353

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...

98-273

6.50e-10

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: 57.82 E-value: 6.50e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  98 IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACaTIDNGTKIGNDTLIKSNVsIAHDVVIG------TGCIIH 171
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDS-TIGDGVVIKASSVIEGAV-IGNGATVGpfahlrPGTVLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 172 QNAVIGcdGFG---NARDEDGSwtKIPQLGRViieDDVEIGSGTTVDRGAI----D-----DTIIKKGARidnlvqiahn 239
Cdd:cd03353   90 EGVHIG--NFVeikKSTIGEGS--KANHLSYL---GDAEIGEGVNIGAGTItcnyDgvnkhRTVIGDNVF---------- 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489115220 240 vvIGRNTALagvtaVAgSTTIGDNCLIGGQSAIT 273
Cdd:cd03353  153 --IGSNSQL-----VA-PVTIGDGATIAAGSTIT 178

LbetaH

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...

108-177

1.14e-09

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: 54.18 E-value: 1.14e-09

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115220 108 AIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTK--IGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIG 177
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGpnEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIG 72

LbH_GlmU_C

cd03353

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...

139-294

7.28e-09

Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 54.73 E-value: 7.28e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 139 TIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGcdgfgnardedgswtkipqlgRVIIEDDVEIGSGT-----T 213
Cdd:cd03353   11 YIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK---------------------DSTIGDGVVIKASSviegaV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 214 VDRGAI--------DDTIIKKGARIDNLVQIAhNVVIGRNTAL------------AGVTAVAGS------------TTIG 261
Cdd:cd03353   70 IGNGATvgpfahlrPGTVLGEGVHIGNFVEIK-KSTIGEGSKAnhlsylgdaeigEGVNIGAGTitcnydgvnkhrTVIG 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489115220 262 DNCLIGGQSAITGHISICDNTIIGGASNIGKSI 294
Cdd:cd03353  149 DNVFIGSNSQLVAPVTIGDGATIAAGSTITKDV 181

WbbJ

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

97-177

9.32e-09

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

Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 53.34 E-value: 9.32e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIA-ASAIIGENVTIGANAVV--GENVVIGDNVYIGACATIDNGT----------KIGNDTLIKSNVSIAHDVV 163
Cdd:COG0110   16 VIGPGVRIYgGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNhpiddpatfpLRTGPVTIGDDVWIGAGAT 95

                         90
                 ....*....|....
gi 489115220 164 IGTGCIIHQNAVIG 177
Cdd:COG0110   96 ILPGVTIGDGAVVG 109

LbH_WxcM_N_like

cd03358

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...

102-177

1.68e-08

Pssm-ID: 100048 [Multi-domain] Cd Length: 119 Bit Score: 52.12 E-value: 1.68e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 102 AVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDN----GTKIGND-----TLIKSNVSIAHDVVIGTGCIIHQ 172
Cdd:cd03358   11 VFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNdlypRSKIYRKwelkgTTVKRGASIGANATILPGVTIGE 90


                 ....*
gi 489115220 173 NAVIG 177
Cdd:cd03358   91 YALVG 95

glmU

PRK14354

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

130-294

2.24e-08

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

Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 55.22 E-value: 2.24e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 130 DNVYIGAcatidnGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIgcdgfGNARDEDGswTKIPQlgRVIIEDdvEIG 209
Cdd:PRK14354 258 ESTYIDA------DVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI-----VDSTIGDG--VTITN--SVIEES--KVG 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 210 SGTTVDRGAI--DDTIIKKGARIDNLVQIaHNVVIGRNTALAGVTAV------------AGS------------TTIGDN 263
Cdd:PRK14354 321 DNVTVGPFAHlrPGSVIGEEVKIGNFVEI-KKSTIGEGTKVSHLTYIgdaevgenvnigCGTitvnydgknkfkTIIGDN 399

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489115220 264 CLIGGQSAITGHISICDNTIIGGASNIGKSI 294
Cdd:PRK14354 400 AFIGCNSNLVAPVTVGDNAYIAAGSTITKDV 430

LbH_MAT_like

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...

109-177

6.86e-08

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: 50.15 E-value: 6.86e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 109 IIGENVTIGANAVV--GENVVIGDNVYIGACATI-------------DNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQN 173
Cdd:cd04647    3 SIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIydhnhdiddperpIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82


                 ....
gi 489115220 174 AVIG 177
Cdd:cd04647   83 AVVG 86

PRK12461

UDP-N-acetylglucosamine acyltransferase; Provisional

97-214

7.37e-08

UDP-N-acetylglucosamine acyltransferase; Provisional

Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 52.72 E-value: 7.37e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGEN------------VVIGDNVYIGACATIDNGTK------IGNDTLIKSNVSI 158
Cdd:PRK12461  37 WIGPHAVILGPTRIGKNNKIHQGAVVGDEpqdftykgeesrLEIGDRNVIREGVTIHRGTKgggvtrIGNDNLLMAYSHV 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489115220 159 AHDVVIGTGCIIHQNAVIGcdgfgnardedgswtkipqlGRVIIEDDVEIGSGTTV 214
Cdd:PRK12461 117 AHDCQIGNNVILVNGALLA--------------------GHVTVGDRAIISGNCLV 152

LbetaH

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...

97-159

1.75e-07

Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 48.01 E-value: 1.75e-07

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGEN--------VVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIA 159
Cdd:cd00208    8 KIHPKAVIRGPVVIGDNVNIGPGAVIGAAtgpneknpTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78

LbH_MAT_like

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...

125-287

1.95e-07

Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 48.61 E-value: 1.95e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 125 NVVIGDNVYIGACATIDNGTK--IGNDTLIKSNVSIahdvvigtgciihqnavigCDGFGNARDEDGSWTKIPQLGRVII 202
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGitIGDNVLIGPNVTI-------------------YDHNHDIDDPERPIEQGVTSAPIVI 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 203 EDDVEIGSGTTVdrgaiddtiikkgaridnlvqiahnvvigrntaLAGVtavagstTIGDNCLIGGQSAITGhiSICDNT 282
Cdd:cd04647   62 GDDVWIGANVVI---------------------------------LPGV-------TIGDGAVVGAGSVVTK--DVPPNS 99


                 ....*
gi 489115220 283 IIGGA 287
Cdd:cd04647  100 IVAGN 104

LbH_SAT

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...

98-162

3.07e-07

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: 47.82 E-value: 3.07e-07

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220  98 IHSKAVIAASAIIGENVTIGANAVVGEN--VVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDV 162
Cdd:cd03354   25 IGETAVIGDNCTIYQGVTLGGKGKGGGKrhPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDV 91

WbbJ

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

155-294

3.27e-07

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

Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 49.10 E-value: 3.27e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 155 NVSIAHDVVIGTGCIIHQNAVIGcdgfgnardedgswtkipqLGRVIIEDDVEIGSGTTVDRGAiddtiikkGARIDNLV 234
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIY-------------------GGNITIGDNVYIGPGVTIDDPG--------GITIGDNV 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115220 235 QIAHNVVIGRNT----ALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSI 294
Cdd:COG0110   55 LIGPGVTILTGNhpidDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDV 118

LbH_Dynactin_5

cd03359

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...

98-176

5.08e-07

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.

Pssm-ID: 100049 [Multi-domain] Cd Length: 161 Bit Score: 48.75 E-value: 5.08e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  98 IHSKAVIAASAII-GE--NVTIGANAVVGENVV------------------IGDNVYIGACATIdNGTKIGNDTLIKSNV 156
Cdd:cd03359   24 LNGKTIIQSDVIIrGDlaTVSIGRYCILSEGCVirppfkkfskgvaffplhIGDYVFIGENCVV-NAAQIGSYVHIGKNC 102

                         90       100
                 ....*....|....*....|
gi 489115220 157 SIAHDVVIGTGCIIHQNAVI 176
Cdd:cd03359  103 VIGRRCIIKDCVKILDGTVV 122

LbH_gamma_CA

cd00710

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...

97-181

5.92e-07

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.

Pssm-ID: 100039 [Multi-domain] Cd Length: 167 Bit Score: 48.78 E-value: 5.92e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGENVVI----GDNVYIGACATIDNGTKI----GNDTLIKSNVSIAHdvvigtGC 168
Cdd:cd00710    4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIradeGTPIIIGANVNIQDGVVIhaleGYSVWIGKNVSIAH------GA 77

                         90
                 ....*....|...
gi 489115220 169 IIHQNAVIGCDGF 181
Cdd:cd00710   78 IVHGPAYIGDNCF 90

GlmU

COG1207

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...

140-292

6.49e-07

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: 50.80 E-value: 6.49e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 140 IDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIgcdgfgnaRDedgswtkipqlgrVIIEDDVEI----GSGTTVD 215
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL--------KD-------------STIGDGVVIkysvIEDAVVG 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 216 RGAI--------DDTIIKKGARIDNLVQIaHNVVIGRNTAL------------AGVTAVAGS------------TTIGDN 263
Cdd:COG1207  322 AGATvgpfarlrPGTVLGEGVKIGNFVEV-KNSTIGEGSKVnhlsyigdaeigEGVNIGAGTitcnydgvnkhrTVIGDG 400

                        170       180
                 ....*....|....*....|....*....
gi 489115220 264 CLIGGQSAITGHISICDNTIIGGASNIGK 292
Cdd:COG1207  401 AFIGSNTNLVAPVTIGDGATIGAGSTITK 429

LbH_G1P_TT_C_like

cd05636

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...

91-230

7.04e-07

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: 48.35 E-value: 7.04e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  91 SPRPDGKIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKS-----NVSIAH----- 160
Cdd:cd05636    7 TVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNsiimdGTKVPHlnyvg 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115220 161 DVVIGTGCIIHQNAVIgcdgfGNARDEDGSWT-----KIPQLGR----VIIEDDVEIGSGTTVDRGaiddTIIKKGARI 230
Cdd:cd05636   87 DSVLGENVNLGAGTIT-----ANLRFDDKPVKvrlkgERVDTGRrklgAIIGDGVKTGINVSLNPG----VKIGPGSWV 156

glmU

PRK14355

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

140-294

7.25e-07

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

Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 50.51 E-value: 7.25e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 140 IDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVI-GCDGFGNARDEDGSwtkipQLGRVIIEDDVEIGSGTTVDRGa 218
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIkGCRIGDDVTVKAGS-----VLEDSVVGDDVAIGPMAHLRPG- 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 219 iddTIIKKGARIDNLVQ----------------------IAHNVVIGRNTALAGVTAVAG-STTIGDNCLIGGQSAITGH 275
Cdd:PRK14355 339 ---TELSAHVKIGNFVEtkkivmgegskashltylgdatIGRNVNIGCGTITCNYDGVKKhRTVIEDDVFVGSDVQFVAP 415

                        170
                 ....*....|....*....
gi 489115220 276 ISICDNTIIGGASNIGKSI 294
Cdd:PRK14355 416 VTVGRNSLIAAGTTVTKDV 434

LbH_G1P_AT_C_like

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...

109-174

7.40e-07

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: 46.47 E-value: 7.40e-07

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115220 109 IIGENVTIGANAVVGeNVVIGDNVYIGACATIDNgTKIGNDTLIKSNVSIaHDVVIGTGCIIHQNA 174
Cdd:cd03356    1 LIGESTVIGENAIIK-NSVIGDNVRIGDGVTITN-SILMDNVTIGANSVI-VDSIIGDNAVIGENV 63

LbH_SAT

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...

104-176

1.92e-06

Pssm-ID: 100045 [Multi-domain] Cd Length: 101 Bit Score: 45.89 E-value: 1.92e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 104 IAASAIIGENVTI--GANAVVGENVVIGDNVYIGACATIDNGT--------KIGNDTLIKSNVSIAHDVVIGTGCIIHQN 173
Cdd:cd03354    5 IHPGAKIGPGLFIdhGTGIVIGETAVIGDNCTIYQGVTLGGKGkgggkrhpTIGDNVVIGAGAKILGNITIGDNVKIGAN 84


                 ...
gi 489115220 174 AVI 176
Cdd:cd03354   85 AVV 87

LbH_G1P_AT_C_like

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...

100-171

1.93e-06

Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 44.93 E-value: 1.93e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115220 100 SKAVIAASAIIGENVTIGANAVVgENVVIGDNVYIGACATIdNGTKIGNDTLIKSNVSIAHDVVIGTGCIIH 171
Cdd:cd03356    9 GENAIIKNSVIGDNVRIGDGVTI-TNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVE 78

Hexapep

pfam00132

Bacterial transferase hexapeptide (six repeats);

107-136

2.28e-06

Bacterial transferase hexapeptide (six repeats);

Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 43.48 E-value: 2.28e-06

                          10        20        30
                  ....*....|....*....|....*....|
gi 489115220  107 SAIIGENVTIGANAVVGENVVIGDNVYIGA 136
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30

CysE

COG1045

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...

103-162

2.60e-06

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis

Pssm-ID: 440667 [Multi-domain] Cd Length: 174 Bit Score: 47.00 E-value: 2.60e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115220 103 VIAASAIIGEN------VTIGANAVVGEN--VVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDV 162
Cdd:COG1045   87 VIGETAVIGDNvtiyqgVTLGGTGKEKGKrhPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDV 154

PLN02296

carbonate dehydratase

84-228

4.22e-06

carbonate dehydratase

Pssm-ID: 215167 [Multi-domain] Cd Length: 269 Bit Score: 47.43 E-value: 4.22e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  84 VMELFDKSPrpdgKIHSKAVIAASA-IIGEnVTIGANAVVGENVVI-GD--NVYIGAcatidnGTKIGNDTLI---KSNV 156
Cdd:PLN02296  45 LMNIFDKAP----VVDKDAFVAPSAsVIGD-VQVGRGSSIWYGCVLrGDvnSISVGS------GTNIQDNSLVhvaKTNL 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115220 157 S-IAHDVVIGTGCIIHQNAVI-GCdgfgnardedgswtkipqlgrvIIEDDVEIGSGTTVdrgaIDDTIIKKGA 228
Cdd:PLN02296 114 SgKVLPTIIGDNVTIGHSAVLhGC----------------------TVEDEAFVGMGATL----LDGVVVEKHA 161

LbH_THP_succinylT

cd03350

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...

113-253

5.25e-06

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: 45.45 E-value: 5.25e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 113 NVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGcdgfGNARDedgswt 192
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIG----GVLEP------ 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115220 193 kiPQLGRVIIEDDVEIGSGTTVDRGaiddTIIKKGAridnlvQIAHNVVIGRNTALAGVTA 253
Cdd:cd03350   71 --LQATPVIIEDDVFIGANCEVVEG----VIVGKGA------VLAAGVVLTQSTPIYDRET 119

glgC

PRK05293

glucose-1-phosphate adenylyltransferase; Provisional

103-159

5.64e-06

glucose-1-phosphate adenylyltransferase; Provisional

Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 47.56 E-value: 5.64e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220 103 VIAASAIIGENVTIgANAVVGENVVIGDNVYIGacATIDNGTKIGNDTLIKSNVSIA 159
Cdd:PRK05293 327 VIMPGAKIGENVVI-ERAIIGENAVIGDGVIIG--GGKEVITVIGENEVIGVGTVIG 380

LbH_Dynactin_5

cd03359

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...

93-165

7.63e-06

Pssm-ID: 100049 [Multi-domain] Cd Length: 161 Bit Score: 45.28 E-value: 7.63e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115220  93 RPDGKIHSKAVIAASAIIGENVTIGANAVV-----GENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIG 165
Cdd:cd03359   58 RPPFKKFSKGVAFFPLHIGDYVFIGENCVVnaaqiGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVS 135

LbH_eIF2B_epsilon

cd05787

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...

103-177

8.52e-06

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: 43.34 E-value: 8.52e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 103 VIAASAIIGENVTIgANAVVGENVVIGDNV-----YIGACATIDNGTKIGNdTLIKSNVSIAHDVVIGTGCIIHQNAVIG 177
Cdd:cd05787    1 VIGRGTSIGEGTTI-KNSVIGRNCKIGKNVvidnsYIWDDVTIEDGCTIHH-SIVADGAVIGKGCTIPPGSLISFGVVIG 78

LbH_paaY_like

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...

119-286

9.01e-06

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: 45.05 E-value: 9.01e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 119 NAVVGENVVIGDNVYIGACATI--DNGTkigndtliksnvsiahdVVIGTGCIIHQNAVIgcDGFgNARDedgswtkipq 196
Cdd:cd04745   12 TAVLIGDVIIGKNCYIGPHASLrgDFGR-----------------IVIRDGANVQDNCVI--HGF-PGQD---------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 197 lgrVIIEDDVEIGSGTtvdrgaiddtiikkgaridnlvqIAHNVVIGRNtALAGVTAVA-GSTTIGDNCLIGGQSAITGH 275
Cdd:cd04745   62 ---TVLEENGHIGHGA-----------------------ILHGCTIGRN-ALVGMNAVVmDGAVIGEESIVGAMAFVKAG 114

                        170
                 ....*....|.
gi 489115220 276 ISICDNTIIGG 286
Cdd:cd04745  115 TVIPPRSLIAG 125

LbH_paaY_like

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...

94-177

1.07e-05

Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 45.05 E-value: 1.07e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  94 PDGKIHSKAVIAASAIIGENVTIGANAVV---GENVVIGDNVYIGACATIDNGtkIGNDTLIKSNVSIAHDVVIgTGCII 170
Cdd:cd04745    5 PSSFVHPTAVLIGDVIIGKNCYIGPHASLrgdFGRIVIRDGANVQDNCVIHGF--PGQDTVLEENGHIGHGAIL-HGCTI 81


                 ....*..
gi 489115220 171 HQNAVIG 177
Cdd:cd04745   82 GRNALVG 88

LbH_MAT_GAT

cd03357

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...

110-286

1.79e-05

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).

Pssm-ID: 100047 [Multi-domain] Cd Length: 169 Bit Score: 44.34 E-value: 1.79e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 110 IGENVTIGANAVV--GENVVIGDNVYIGACATI--DNGTKIGNDTLIKSNVSI---AH--DVVigtgciihqnavigcdg 180
Cdd:cd03357   45 VGENVYIEPPFHCdyGYNIHIGDNFYANFNCTIldVAPVTIGDNVLIGPNVQIytaGHplDPE----------------- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 181 fgnARDEDGSWTKiPqlgrVIIEDDVEIGSGTTVdrgaiddtiikkgaridnlvqiahnvvigrntaLAGVtavagstTI 260
Cdd:cd03357  108 ---ERNRGLEYAK-P----ITIGDNVWIGGGVII---------------------------------LPGV-------TI 139

                        170       180
                 ....*....|....*....|....*.
gi 489115220 261 GDNCLIGGQSAITGhiSICDNTIIGG 286
Cdd:cd03357  140 GDNSVIGAGSVVTK--DIPANVVAAG 163

LbH_SAT

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...

206-294

2.07e-05

Pssm-ID: 100045 [Multi-domain] Cd Length: 101 Bit Score: 42.81 E-value: 2.07e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 206 VEIGSGTTVDRG-AID---DTIIKKGARIDNLVQIAHNVVIGRNtalaGVTAVAGSTTIGDNCLIGGQSAITGHISICDN 281
Cdd:cd03354    3 IDIHPGAKIGPGlFIDhgtGIVIGETAVIGDNCTIYQGVTLGGK----GKGGGKRHPTIGDNVVIGAGAKILGNITIGDN 78

                         90
                 ....*....|...
gi 489115220 282 TIIGGASNIGKSI 294
Cdd:cd03354   79 VKIGANAVVTKDV 91

LbH_G1P_TT_C_like

cd05636

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...

97-267

2.30e-05

Pssm-ID: 100060 [Multi-domain] Cd Length: 163 Bit Score: 44.12 E-value: 2.30e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGAcatidnGTKIGNDTLIKSNVSIAHDVVIGTGCIIhQNAVI 176
Cdd:cd05636    1 KDEIEGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGK------GCEIGPNAYIRGYTVLGDGCVVGNSVEV-KNSII 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 177 GcDGfgnardedgswTKIPQLGRV---IIEDDVEIGSGTTVDRGAIDDTIIK---KGARIDNLVQ-----IAHNVVIGRN 245
Cdd:cd05636   74 M-DG-----------TKVPHLNYVgdsVLGENVNLGAGTITANLRFDDKPVKvrlKGERVDTGRRklgaiIGDGVKTGIN 141

                        170       180
                 ....*....|....*....|..
gi 489115220 246 TALAGVTAVAGSTTIGDNCLIG 267
Cdd:cd05636  142 VSLNPGVKIGPGSWVYPGCVVR 163

glmU

PRK14356

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

111-273

2.47e-05

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

Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 45.87 E-value: 2.47e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 111 GENVTIGANAVVGENVVIgdnvyIGACaTIDNGTKIGNDTLIKSNVSIaHDVVIGTGCIIH-----QNAVIGCDG----F 181
Cdd:PRK14356 261 PESVRIGPRATIEPGAEI-----YGPC-EIYGASRIARGAVIHSHCWL-RDAVVSSGATIHsfshlEGAEVGDGCsvgpY 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 182 GNARD----EDGSW------TKIPQLGR------VIIEDDVEIGSGTTVDRGAIddTIIKKGARiDNLVQIAHNVVIGRN 245
Cdd:PRK14356 334 ARLRPgavlEEGARvgnfveMKKAVLGKgakanhLTYLGDAEIGAGANIGAGTI--TCNYDGVN-KHRTVIGEGAFIGSN 410

                        170       180
                 ....*....|....*....|....*...
gi 489115220 246 TALagvtaVAgSTTIGDNCLIGGQSAIT 273
Cdd:PRK14356 411 TAL-----VA-PVTIGDGALVGAGSVIT 432

NRPS_term_dom

TIGR02353

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...

143-242

2.68e-05

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.

Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 45.90 E-value: 2.68e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  143 GTKIGNDTLIKSNVSIAHDVV-IGTGCIIHQNAVigcdgFGNARDEDGswtkIPQLGRVIIEDDVEIGSGTTVDRgaidD 221
Cdd:TIGR02353 112 GAKIGKGVDIGSLPPVCTDLLtIGAGTIVRKEVM-----LLGYRAERG----RLHTGPVTLGRDAFIGTRSTLDI----D 178

                          90       100
                  ....*....|....*....|.
gi 489115220  222 TIIKKGARIDNLVQIAHNVVI 242
Cdd:TIGR02353 179 TSIGDGAQLGHGSALQGGQSI 199

LbH_eIF2B_epsilon

cd05787

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...

140-244

4.97e-05

Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 41.02 E-value: 4.97e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 140 IDNGTKIGNDTLIKSNVsiahdvvIGTGCIIHQNAVIgcdgfgnardeDGSWtkipqlgrviIEDDVEIGSGTTVDRGAI 219
Cdd:cd05787    2 IGRGTSIGEGTTIKNSV-------IGRNCKIGKNVVI-----------DNSY----------IWDDVTIEDGCTIHHSIV 53

                         90       100
                 ....*....|....*....|....*.
gi 489115220 220 -DDTIIKKGARIDNLVQIAHNVVIGR 244
Cdd:cd05787   54 aDGAVIGKGCTIPPGSLISFGVVIGD 79

WbbJ

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

98-162

5.08e-05

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

Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 42.55 E-value: 5.08e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  98 IHSKAVIAASA--IIGENVTIGANAVV----------------GENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIA 159
Cdd:COG0110   36 IGPGVTIDDPGgiTIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVT 115


                 ...
gi 489115220 160 HDV 162
Cdd:COG0110  116 KDV 118

LbH_THP_succinylT

cd03350

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...

94-177

6.76e-05

Pssm-ID: 100041 [Multi-domain] Cd Length: 139 Bit Score: 42.37 E-value: 6.76e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  94 PDGKIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGND--------------TLIKSNVSIA 159
Cdd:cd03350    6 PGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGaviggvleplqatpVIIEDDVFIG 85

                         90
                 ....*....|....*...
gi 489115220 160 HDVVIGTGCIIHQNAVIG 177
Cdd:cd03350   86 ANCEVVEGVIVGKGAVLA 103

glmU

PRK14355

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

94-254

6.88e-05

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

Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 44.35 E-value: 6.88e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  94 PDGKIHSKAVIAASAIIGENVTIGANAVVgENVVIGDNVYIGAcATIDNGTKIGNDTLI------KSNVSIAHDVVIGTg 167
Cdd:PRK14355 273 RDTTIYPGVCISGDTRIGEGCTIEQGVVI-KGCRIGDDVTVKA-GSVLEDSVVGDDVAIgpmahlRPGTELSAHVKIGN- 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 168 CIIHQNAVIGcdgfgnardEDGSWTKIPQLGRVIIEDDVEIGSGTTV---DRGAIDDTIIKKGARIDNLVQIAHNVVIGR 244
Cdd:PRK14355 350 FVETKKIVMG---------EGSKASHLTYLGDATIGRNVNIGCGTITcnyDGVKKHRTVIEDDVFVGSDVQFVAPVTVGR 420

                        170
                 ....*....|
gi 489115220 245 NTALAGVTAV 254
Cdd:PRK14355 421 NSLIAAGTTV 430

LbH_paaY_like

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...

104-152

7.40e-05

Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 42.36 E-value: 7.40e-05

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489115220 104 IAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLI 152
Cdd:cd04745   75 ILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLI 123

LbH_MAT_like

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...

199-294

8.74e-05

Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 41.29 E-value: 8.74e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 199 RVIIEDDVEIGSGTTVDRGaiddtiikKGARIDNLVQIAHNVVI-------GRNTALAGVTAVAGSTTIGDNCLIGGQSA 271
Cdd:cd04647    1 NISIGDNVYIGPGCVISAG--------GGITIGDNVLIGPNVTIydhnhdiDDPERPIEQGVTSAPIVIGDDVWIGANVV 72

                         90       100
                 ....*....|....*....|...
gi 489115220 272 ITGHISICDNTIIGGASNIGKSI 294
Cdd:cd04647   73 ILPGVTIGDGAVVGAGSVVTKDV 95

glmU

PRK14357

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

140-294

9.30e-05

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

Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 43.98 E-value: 9.30e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 140 IDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNARDEDGSwtkipQLGRVIIEDDVEIGSGTTVDRGai 219
Cdd:PRK14357 252 IHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKIIRS-----ECEKSVIEDDVSVGPFSRLREG-- 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 220 ddTIIKKGARIDNLVQIAhNVVIGRNT----------ALAG--VTAVAGSTT------------IGDNCLIGGQSAITGH 275
Cdd:PRK14357 325 --TVLKKSVKIGNFVEIK-KSTIGENTkaqhltylgdATVGknVNIGAGTITcnydgkkknptfIEDGAFIGSNSSLVAP 401

                        170
                 ....*....|....*....
gi 489115220 276 ISICDNTIIGGASNIGKSI 294
Cdd:PRK14357 402 VRIGKGALIGAGSVITEDV 420

LbH_M1P_guanylylT_C

cd05824

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...

103-179

9.58e-05

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: 40.21 E-value: 9.58e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220 103 VIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTkIGNDTLIKSNVsIAHDVVIGTGCIIHQNAVIGCD 179
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNST-VRDHSWVKSSI-VGWNSTVGRWTRLENVTVLGDD 75

glmU

PRK09451

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

111-261

1.02e-04

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

Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 43.86 E-value: 1.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 111 GENVTIGANAVVGENVVIGDNVYIGACATIDNGTkIGNDTLIKSnVSIAHDVVIGTGCII------------HQNAVIGc 178
Cdd:PRK09451 269 GRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCV-IGDDCEISP-YSVVEDANLGAACTIgpfarlrpgaelAEGAHVG- 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 179 dGF---GNARDEDGSwtKIPQLGRViieDDVEIGSGTTVDRGAIddTIIKKGARIDNLVqIAHNVVIGRNTALAGVTAVA 255
Cdd:PRK09451 346 -NFvemKKARLGKGS--KAGHLTYL---GDAEIGDNVNIGAGTI--TCNYDGANKFKTI-IGDDVFVGSDTQLVAPVTVG 416


                 ....*.
gi 489115220 256 GSTTIG 261
Cdd:PRK09451 417 KGATIG 422

PaaY

COG0663

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...

108-146

1.23e-04

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];

Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 41.94 E-value: 1.23e-04

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489115220 108 AIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKI 146
Cdd:COG0663   89 CTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVV 127

GlgC

COG0448

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...

85-246

1.23e-04

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

Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 43.53 E-value: 1.23e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  85 MELFDKSPR-----PDGKIHSKAVIAASAIIGENVTIgANAVVG---------ENVVIGDNVYIGACATIDNgtkigndt 150
Cdd:COG0448  250 MDLLDPEPEfnlydPEWPIYTKQKDLPPAKFVRGGKV-KNSLVSngciisgtvENSVLFRGVRVESGAVVEN-------- 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 151 liksnvsiahdvvigtgCIIHQNAVIGcdgfgnardeDGSwtkipQLGRVIIEDDVEIGSGTTVdrGAIDDTIIKKGARI 230
Cdd:COG0448  321 -----------------SVIMPGVVIG----------EGA-----VIENAIIDKNVVIPPGVVI--GEDPEEDRKRFTVS 366

                        170
                 ....*....|....*.
gi 489115220 231 DNLvqiahnVVIGRNT 246
Cdd:COG0448  367 SGI------VVVGKGA 376

LbH_paaY_like

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...

197-288

1.48e-04

Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 41.58 E-value: 1.48e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 197 LGRVIIEDDVEIGSGTTVdRGAIDDTIIKKGARI-DNLV---QIAHNVVIGRNTALaGVTAVAGSTTIGDNCLIGGQSAI 272
Cdd:cd04745   16 IGDVIIGKNCYIGPHASL-RGDFGRIVIRDGANVqDNCVihgFPGQDTVLEENGHI-GHGAILHGCTIGRNALVGMNAVV 93

                         90
                 ....*....|....*.
gi 489115220 273 TGHISICDNTIIGGAS 288
Cdd:cd04745   94 MDGAVIGEESIVGAMA 109

DapD

COG2171

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...

105-146

1.54e-04

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis

Pssm-ID: 441774 [Multi-domain] Cd Length: 268 Bit Score: 42.80 E-value: 1.54e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489115220 105 AASAIIGENVTIGANA------VVGENVVIGDNVYIGAcatidnGTKI 146
Cdd:COG2171  168 AAPVIIEDNCFIGARSgvvegvIVGEGAVLGAGVYLTA------STKI 209

LbH_LpxD

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...

104-162

1.61e-04

Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 42.01 E-value: 1.61e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115220 104 IAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDV 162
Cdd:cd03352  129 IAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIV 187

LbH_gamma_CA

cd00710

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...

163-270

1.93e-04

Pssm-ID: 100039 [Multi-domain] Cd Length: 167 Bit Score: 41.46 E-value: 1.93e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 163 VIGTGCIIHQNAVIgcdgfgnardedgswtkipqLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQI----AH 238
Cdd:cd00710    4 VIDPSAYVHPTAVV--------------------IGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIhaleGY 63

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489115220 239 NVVIGRNTALAGVTAVAGSTTIGDNCLIGGQS 270
Cdd:cd00710   64 SVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRS 95

LbH_Dynactin_6

cd04646

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...

145-289

2.16e-04

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.

Pssm-ID: 100052 [Multi-domain] Cd Length: 164 Bit Score: 41.16 E-value: 2.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 145 KIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCD------GFGNardedgswtkipqlgrvIIEDDVEIGSGTTVDRGA 218
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEagpiiiGENN-----------------IIEEQVTIVNKKPKDPAE 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115220 219 IDDTIIkkGAriDNLVQI---AHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASN 289
Cdd:cd04646   64 PKPMII--GS--NNVFEVgckCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADC 133

Hexapep

pfam00132

Bacterial transferase hexapeptide (six repeats);

143-171

2.34e-04

Bacterial transferase hexapeptide (six repeats);

Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 37.70 E-value: 2.34e-04

                          10        20
                  ....*....|....*....|....*....
gi 489115220  143 GTKIGNDTLIKSNVSIAHDVVIGTGCIIH 171
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29

LbH_G1P_AT_C_like

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...

97-153

2.57e-04

Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 39.15 E-value: 2.57e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220  97 KIHSKAVIAASaIIGENVTIGANAVVgENVVIGDNVYIGACATIDNGTKIGNDTLIK 153
Cdd:cd03356   24 RIGDGVTITNS-ILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVE 78

LbH_unknown

cd05635

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...

114-214

3.30e-04

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain] Cd Length: 101 Bit Score: 39.57 E-value: 3.30e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 114 VTIGANAVVGENVVIGDNVYIGACATIDNGTKigndtlIKSNVSIAHDVVIG---TGCIIHQNAVIGCDGFgnardedgs 190
Cdd:cd05635   12 IYIGKDAVIEPFAVIEGPVYIGPGSRVKMGAR------IYGNTTIGPTCKIGgevEDSIIEGYSNKQHDGF--------- 76

                         90       100
                 ....*....|....*....|....
gi 489115220 191 wtkipqLGRVIIEDDVEIGSGTTV 214
Cdd:cd05635   77 ------LGHSYLGSWCNLGAGTNN 94

LbH_XAT

cd03349

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...

125-219

3.30e-04

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.

Pssm-ID: 100040 [Multi-domain] Cd Length: 145 Bit Score: 40.22 E-value: 3.30e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 125 NVVIGDNVYIG--ACATIDNGTKIGNDtliksnVSIAHDVVIGTGCI--IHQNAVIGCDGFGNARDEDGSWTKIPQLGRV 200
Cdd:cd03349    1 NISVGDYSYGSgpDCDVGGDKLSIGKF------CSIAPGVKIGLGGNhpTDWVSTYPFYIFGGEWEDDAKFDDWPSKGDV 74

                         90       100
                 ....*....|....*....|....*
gi 489115220 201 IIEDDVEIG------SGTTVDRGAI 219
Cdd:cd03349   75 IIGNDVWIGhgatilPGVTIGDGAV 99

PLN02694

serine O-acetyltransferase

79-179

3.74e-04

serine O-acetyltransferase

Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 41.55 E-value: 3.74e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  79 MALA---KVMELFDKSPRPDGKIhSKAVIAASAIigeNVTIGANAVVGENVVIGDNVYIGAC--ATIDNGTKIGNDTLIK 153
Cdd:PLN02694 147 LALAlhsRISDVFAVDIHPAAKI-GKGILFDHAT---GVVIGETAVIGNNVSILHHVTLGGTgkACGDRHPKIGDGVLIG 222

                         90       100
                 ....*....|....*....|....*.
gi 489115220 154 SNVSIAHDVVIGTGCIIHQNAVIGCD 179
Cdd:PLN02694 223 AGATILGNVKIGEGAKIGAGSVVLID 248

LbH_LpxD

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...

98-136

3.80e-04

Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 40.85 E-value: 3.80e-04

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489115220  98 IHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGA 136
Cdd:cd03352  141 IAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGA 179

glgC

PRK05293

glucose-1-phosphate adenylyltransferase; Provisional

109-177

5.46e-04

glucose-1-phosphate adenylyltransferase; Provisional

Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 41.39 E-value: 5.46e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115220 109 IIGENVTIGANAVVGE-----NVVIGDNVYIGAcATIDNGTKIGNDTLIKSNVSIAhdVVIGTGCIIHQNAVIG 177
Cdd:PRK05293 310 VLFQGVQVGEGSVVKDsvimpGAKIGENVVIER-AIIGENAVIGDGVIIGGGKEVI--TVIGENEVIGVGTVIG 380

LbH_G1P_AT_C_like

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...

146-244

5.97e-04

Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 37.99 E-value: 5.97e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 146 IGNDTLIKSNVSIAHdVVIGTGCIIHQNAVIgcdgfgnardeDGSwtkipqlgrvIIEDDVEIGSGTTVDRGAIDD-TII 224
Cdd:cd03356    2 IGESTVIGENAIIKN-SVIGDNVRIGDGVTI-----------TNS----------ILMDNVTIGANSVIVDSIIGDnAVI 59

                         90       100
                 ....*....|....*....|
gi 489115220 225 KKGARIDNLVQIAHNVVIGR 244
Cdd:cd03356   60 GENVRVVNLCIIGDDVVVED 79

glgC

PRK05293

glucose-1-phosphate adenylyltransferase; Provisional

85-211

7.19e-04

glucose-1-phosphate adenylyltransferase; Provisional

Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 41.01 E-value: 7.19e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  85 MELFDKSPR-----PDGKIHSKAVIAASAIIGENVTIgANAVVGENVVIGDNVYigaCATIDNGTKIGNDTLIKSNVsIA 159
Cdd:PRK05293 255 MELLRPENPlnlfdRNWRIYSVNPNLPPQYIAENAKV-KNSLVVEGCVVYGTVE---HSVLFQGVQVGEGSVVKDSV-IM 329

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489115220 160 HDVVIGTGCIIHqNAVIGCDgfgnardedgswtkipqlgrVIIEDDVEIGSG 211
Cdd:PRK05293 330 PGAKIGENVVIE-RAIIGEN--------------------AVIGDGVIIGGG 360

LbH_FBP

cd04650

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...

110-176

7.64e-04

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.

Pssm-ID: 100055 [Multi-domain] Cd Length: 154 Bit Score: 39.48 E-value: 7.64e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220 110 IGENVTIGANAVVgENVVIGDNVYIGACATIDNGTKIGNdtliksnvsiahDVVIGTGCIIHQNAVI 176
Cdd:cd04650   64 IGDYVTIGHNAVV-HGAKVGNYVIVGMGAILLNGAKIGD------------HVIIGAGAVVTPGKEI 117

DapD

COG2171

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...

102-177

7.64e-04

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis

Pssm-ID: 441774 [Multi-domain] Cd Length: 268 Bit Score: 40.49 E-value: 7.64e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 102 AVIAASAIIGENVT-------IGA----------NAVVGENVVIGDNVYIGACATI--------DNGTKIGNDTLIKSNV 156
Cdd:COG2171  104 ARVRLGAYLAPGVVlmpsfvnIGAyvdegtmvdtWATVGSCAQIGKNVHLSGGAGIggvleplqAAPVIIEDNCFIGARS 183

                         90       100
                 ....*....|....*....|.
gi 489115220 157 SIAHDVVIGTGCIIHQNAVIG 177
Cdd:COG2171  184 GVVEGVIVGEGAVLGAGVYLT 204

glmU

PRK14360

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

114-292

8.13e-04

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

Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 41.07 E-value: 8.13e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 114 VTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKsnvsiahDVVIGTGCIIHQNAVIGCDgfgnardedgswtk 193
Cdd:PRK14360 257 CTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIE-------NSQIGENVTVLYSVVSDSQ-------------- 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 194 ipqlgrviIEDDVEIGSGTTVdRGAIDdtiIKKGARIDNLVQI-----------AHNVVIGRNTALAGVTAVAGS----- 257
Cdd:PRK14360 316 --------IGDGVKIGPYAHL-RPEAQ---IGSNCRIGNFVEIkksqlgegskvNHLSYIGDATLGEQVNIGAGTitany 383

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489115220 258 -------TTIGDNCLIGGQSAITGHISICDNTIIGGASNIGK 292
Cdd:PRK14360 384 dgvkkhrTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITK 425

PRK10191

putative acyl transferase; Provisional

104-170

8.54e-04

putative acyl transferase; Provisional

Pssm-ID: 182295 [Multi-domain] Cd Length: 146 Bit Score: 39.10 E-value: 8.54e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 104 IAASAIIGENVTI--GANAVVGENVVIGDN------VYIG-------ACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGC 168
Cdd:PRK10191  44 IQAAATIGRRFTIhhGYAVVINKNVVAGDDftirhgVTIGnrgadnmACPHIGNGVELGANVIILGDITIGNNVTVGAGS 123


                 ..
gi 489115220 169 II 170
Cdd:PRK10191 124 VV 125

LbH_MAT_like

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...

88-138

9.80e-04

Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 38.21 E-value: 9.80e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489115220  88 FDKSPRPDGKIHSKAVIaasaIIGENVTIGANAVVGENVVIGDNVYIGACA 138
Cdd:cd04647   43 IDDPERPIEQGVTSAPI----VIGDDVWIGANVVILPGVTIGDGAVVGAGS 89

PLN02357

serine acetyltransferase

206-294

1.14e-03

serine acetyltransferase

Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 40.25 E-value: 1.14e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 206 VEIGSGTTVDRGAIDD----TIIKKGARIDNLVQIAHNVVIGrntalaGVTAVAGS--TTIGDNCLIGGQSAITGHISIC 279
Cdd:PLN02357 227 VDIHPGAKIGQGILLDhatgVVIGETAVVGNNVSILHNVTLG------GTGKQSGDrhPKIGDGVLIGAGTCILGNITIG 300

                         90
                 ....*....|....*
gi 489115220 280 DNTIIGGASNIGKSI 294
Cdd:PLN02357 301 EGAKIGAGSVVLKDV 315

LbH_AT_putative

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...

95-148

1.28e-03

Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 39.39 E-value: 1.28e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115220  95 DGKIHSKAVIAASAIIGENVTIGANAVVG------ENVVIGDNVYIGACATI-----DNGTKIGN 148
Cdd:cd03360  132 DCVIGDFVHIAPGVVLSGGVTIGEGAFIGagatiiQGVTIGAGAIIGAGAVVtkdvpDGSVVVGN 196

PLN02694

serine O-acetyltransferase

192-288

1.40e-03

serine O-acetyltransferase

Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 40.01 E-value: 1.40e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 192 TKIPQLGRVIIEDDVEIGSGTTVDRGAidDTIIKKGARIDNLVQIAHNVVIGrntalaGVTAVAGS--TTIGDNCLIGGQ 269
Cdd:PLN02694 153 SRISDVFAVDIHPAAKIGKGILFDHAT--GVVIGETAVIGNNVSILHHVTLG------GTGKACGDrhPKIGDGVLIGAG 224

                         90
                 ....*....|....*....
gi 489115220 270 SAITGHISICDNTIIGGAS 288
Cdd:PLN02694 225 ATILGNVKIGEGAKIGAGS 243

PRK10092

maltose O-acetyltransferase; Provisional

123-162

1.40e-03

maltose O-acetyltransferase; Provisional

Pssm-ID: 182235 [Multi-domain] Cd Length: 183 Bit Score: 39.03 E-value: 1.40e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489115220 123 GENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDV 162
Cdd:PRK10092 127 GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDV 166

LbetaH

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...

145-237

1.45e-03

Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 36.84 E-value: 1.45e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 145 KIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNardedgswtkipQLGRVIIEDDVEIGSGTTVDRGAiddtII 224
Cdd:cd00208    2 FIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN------------EKNPTIIGDNVEIGANAVIHGGV----KI 65

                         90
                 ....*....|...
gi 489115220 225 KKGARIDNLVQIA 237
Cdd:cd00208   66 GDNAVIGAGAVVT 78

dapD

PRK11830

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional

105-146

1.66e-03

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional

Pssm-ID: 236996 [Multi-domain] Cd Length: 272 Bit Score: 39.40 E-value: 1.66e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489115220 105 AASAIIGENVTIGAN------AVVGENVVIGDNVYIGAcatidnGTKI 146
Cdd:PRK11830 174 ANPVIIEDNCFIGARsevvegVIVEEGSVLGMGVFLGQ------STKI 215

PLN02739

serine acetyltransferase

98-176

1.84e-03

serine acetyltransferase

Pssm-ID: 215394 [Multi-domain] Cd Length: 355 Bit Score: 39.63 E-value: 1.84e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  98 IHSKAVIAASAII--GENVTIGANAVVGENVVIGDNVYIGACA--TIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQN 173
Cdd:PLN02739 208 IHPAARIGKGILLdhGTGVVIGETAVIGDRVSILHGVTLGGTGkeTGDRHPKIGDGALLGACVTILGNISIGAGAMVAAG 287


                 ...
gi 489115220 174 AVI 176
Cdd:PLN02739 288 SLV 290

LbH_SAT

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...

132-230

2.24e-03

Pssm-ID: 100045 [Multi-domain] Cd Length: 101 Bit Score: 37.03 E-value: 2.24e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 132 VYIGACATIDNGTKIGNDTliksNVSIAHDVVIGTGCIIHQNAVIGCDGFGNardedgswtkipQLGRVIIEDDVEIGSG 211
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGT----GIVIGETAVIGDNCTIYQGVTLGGKGKGG------------GKRHPTIGDNVVIGAG 66

                         90
                 ....*....|....*....
gi 489115220 212 TTVdrgaIDDTIIKKGARI 230
Cdd:cd03354   67 AKI----LGNITIGDNVKI 81

Hexapep

pfam00132

Bacterial transferase hexapeptide (six repeats);

119-148

2.70e-03

Bacterial transferase hexapeptide (six repeats);

Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 35.01 E-value: 2.70e-03

                          10        20        30
                  ....*....|....*....|....*....|
gi 489115220  119 NAVVGENVVIGDNVYIGACATIDNGTKIGN 148
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30

LbH_G1P_TT_C_like

cd05636

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...

229-294

3.14e-03

Pssm-ID: 100060 [Multi-domain] Cd Length: 163 Bit Score: 37.95 E-value: 3.14e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115220 229 RIDNLVQIAHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSI 294
Cdd:cd05636    7 TVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI 72

glmU

PRK14353

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

144-299

3.18e-03

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

Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 39.07 E-value: 3.18e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 144 TKIGNDTLIKSNVSIAHDVVIGTGCIIH-----------QNAVIGcdgfGNARDEDGSwtkipqlgrvIIEDDVEIGSGT 212
Cdd:PRK14353 269 TVIGRDVVIEPNVVFGPGVTVASGAVIHafshlegahvgEGAEVG----PYARLRPGA----------ELGEGAKVGNFV 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 213 TVDRGAIDdtiikKGARIDNLVQIAhNVVIGrntalAGVTAVAGS------------TTIGDNCLIGGQSAITGHISICD 280
Cdd:PRK14353 335 EVKNAKLG-----EGAKVNHLTYIG-DATIG-----AGANIGAGTitcnydgfnkhrTEIGAGAFIGSNSALVAPVTIGD 403

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489115220 281 NTIIGGASNI-------------GKSITKPGM 299
Cdd:PRK14353 404 GAYIASGSVItedvpddalalgrARQETKPGW 435

LbH_THP_succinylT

cd03350

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...

201-294

3.22e-03

Pssm-ID: 100041 [Multi-domain] Cd Length: 139 Bit Score: 37.36 E-value: 3.22e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 201 IIEDDVEIGSGTTVDRGAI--------DDTIIKKGARIDNLVQIAHNVVIGRNTALAGVT--AVAGSTTIGDNCLIGGQS 270
Cdd:cd03350    9 IIRDGAFIGPGAVLMMPSYvnigayvdEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLepLQATPVIIEDDVFIGANC 88

                         90       100
                 ....*....|....*....|....
gi 489115220 271 AITGHISICDNTIIGGASNIGKSI 294
Cdd:cd03350   89 EVVEGVIVGKGAVLAAGVVLTQST 112

PLN02357

serine acetyltransferase

114-176

3.85e-03

serine acetyltransferase

Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 38.71 E-value: 3.85e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115220 114 VTIGANAVVGENVVIGDNVYIGACATI--DNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVI 176
Cdd:PLN02357 247 VVIGETAVVGNNVSILHNVTLGGTGKQsgDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVV 311

LbH_Dynactin_6

cd04646

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...

97-176

4.01e-03

Pssm-ID: 100052 [Multi-domain] Cd Length: 164 Bit Score: 37.30 E-value: 4.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220  97 KIHSKAVIAASAIIGENVTIGANAVVGEN---------VVIGDNVYIGACATIDNGT----------------------- 144
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRatiiaeagpIIIGENNIIEEQVTIVNKKpkdpaepkpmiigsnnvfevgck 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489115220 145 ----KIGNDTLIKS------NVSIAHDVVIGTGCIIHQNAVI 176
Cdd:cd04646   81 cealKIGNNNVFESksfvgkNVIITDGCIIGAGCKLPSSEIL 122

LbH_eIF2B_gamma_C

cd04652

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...

103-177

4.16e-03

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: 35.63 E-value: 4.16e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115220 103 VIAASAIIGENVTIgANAVVGENVVIGDNVYIGACatidngtkigndtLIKSNVSIAHDVVIgTGCIIHQNAVIG 177
Cdd:cd04652    1 LVGENTQVGEKTSI-KRSVIGANCKIGKRVKITNC-------------VIMDNVTIEDGCTL-ENCIIGNGAVIG 60

Hexapep_2

pfam14602

Hexapeptide repeat of succinyl-transferase;

109-141

5.59e-03

Hexapeptide repeat of succinyl-transferase;

Pssm-ID: 434064 [Multi-domain] Cd Length: 33 Bit Score: 33.95 E-value: 5.59e-03

                          10        20        30
                  ....*....|....*....|....*....|...
gi 489115220  109 IIGENVTIGANAVVGenVVIGDNVYIGACATID 141
Cdd:pfam14602   2 IIGDNCLIGANSGIG--VSLGDNCVVGAGVVIT 32

glmU

PRK14353

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

115-273

6.16e-03

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

Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 38.30 E-value: 6.16e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 115 TIGANAVVGENVVIGDNVYIGACATID-----NGTKIGNDTLI------KSNVSIAHDVVIGTGCIIhQNAVIGcdgfgn 183
Cdd:PRK14353 270 VIGRDVVIEPNVVFGPGVTVASGAVIHafshlEGAHVGEGAEVgpyarlRPGAELGEGAKVGNFVEV-KNAKLG------ 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 184 ardeDGSwtKIPQLGRViieDDVEIGSGTTVDRGAID---DTIIKKGARIDNlvqiahNVVIGRNTALagVTAVagstTI 260
Cdd:PRK14353 343 ----EGA--KVNHLTYI---GDATIGAGANIGAGTITcnyDGFNKHRTEIGA------GAFIGSNSAL--VAPV----TI 401

                        170
                 ....*....|...
gi 489115220 261 GDNCLIGGQSAIT 273
Cdd:PRK14353 402 GDGAYIASGSVIT 414

PRK09677

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional

122-286

7.60e-03

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional

Pssm-ID: 137467 [Multi-domain] Cd Length: 192 Bit Score: 37.16 E-value: 7.60e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 122 VGENVVIGDNVYIGACATIdngtKIGNDTLIKSNVSIAhdvvigtgciihqnavigcdgfgnarDEDGSWTKIPqlgrvi 201
Cdd:PRK09677  68 FGDNVQVNDYVHIACIESI----TIGRDTLIASKVFIT--------------------------DHNHGSFKHS------ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 202 ieDDVEIGSGTTVDRGAIDDTIIkkgaridnlvqIAHNVVIGRNtalagVTAVAGsTTIGDNCLIGGQSAITGhiSICDN 281
Cdd:PRK09677 112 --DDFSSPNLPPDMRTLESSAVV-----------IGQRVWIGEN-----VTILPG-VSIGNGCIVGANSVVTK--SIPEN 170


                 ....*
gi 489115220 282 TIIGG 286
Cdd:PRK09677 171 TVIAG 175

LbH_unknown

cd05635

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...

223-289

7.65e-03

Pssm-ID: 100059 [Multi-domain] Cd Length: 101 Bit Score: 35.33 E-value: 7.65e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220 223 IIKKGARIDNLVQIAHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQsaitghisiCDNTIIGGASN 289
Cdd:cd05635   13 YIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIGGE---------VEDSIIEGYSN 70

DapD

COG2171

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...

208-296

7.94e-03

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis

Pssm-ID: 441774 [Multi-domain] Cd Length: 268 Bit Score: 37.40 E-value: 7.94e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 208 IGSGTTVDRGAIddtiIKKGARIDNLVQIAHNVVIGrnTALAGVTAVagSTTIGDNCLIGGQSAITGHISICDNTIIGGA 287
Cdd:COG2171  129 VDEGTMVDTWAT----VGSCAQIGKNVHLSGGAGIG--GVLEPLQAA--PVIIEDNCFIGARSGVVEGVIVGEGAVLGAG 200


                 ....*....
gi 489115220 288 SNIGKSiTK 296
Cdd:COG2171  201 VYLTAS-TK 208

LbH_MAT_like

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...

98-152

8.12e-03

Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 35.51 E-value: 8.12e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115220  98 IHSKAVIAASA--IIGENVTIGANA-------------------VVGENVVIGDNVYIGACATIDNGTKIGNDTLI 152
Cdd:cd04647   10 IGPGCVISAGGgiTIGDNVLIGPNVtiydhnhdiddperpieqgVTSAPIVIGDDVWIGANVVILPGVTIGDGAVV 85

glmU

PRK09451

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...

139-318

8.60e-03

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

Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 37.70 E-value: 8.60e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 139 TIDNGTKIGNDT--LIKSNVSIAHDVVIGTGCIIhQNAVIGCDgfgnardedgswtkipqlgrVIIE-----DDVEIGSG 211
Cdd:PRK09451 265 TLTHGRDVEIDTnvIIEGNVTLGNRVKIGAGCVL-KNCVIGDD--------------------CEISpysvvEDANLGAA 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115220 212 TTV------------DRGA-------IDDTIIKKGARIDNL-----VQIAHNVVIGrntalAGVT------AVAGSTTIG 261
Cdd:PRK09451 324 CTIgpfarlrpgaelAEGAhvgnfveMKKARLGKGSKAGHLtylgdAEIGDNVNIG-----AGTItcnydgANKFKTIIG 398

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489115220 262 DNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMYYAAFEAKPRIQWGRFVAK 318
Cdd:PRK09451 399 DDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGWQRPVKK 455

LbetaH