NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446462099|ref|WP_000539953|]
View 

serine O-acetyltransferase [Streptococcus pneumoniae]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568
SCOP:  4001889

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 6-173 2.19e-76

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: 226.89  E-value: 2.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   6 ETIDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLARMHSQFWRFWTQIEIHPGAQIDSGVFIDHGSGL 85
Cdd:COG1045    7 EDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  86 VIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAK 165
Cdd:COG1045   87 VIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPAR 166


                 ....*...
gi 446462099 166 IVRLHGKK 173
Cdd:COG1045  167 IVKRKGSK 174
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 6-173 2.19e-76

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: 226.89  E-value: 2.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   6 ETIDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLARMHSQFWRFWTQIEIHPGAQIDSGVFIDHGSGL 85
Cdd:COG1045    7 EDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  86 VIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAK 165
Cdd:COG1045   87 VIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPAR 166


                 ....*...
gi 446462099 166 IVRLHGKK 173
Cdd:COG1045  167 IVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 6-165 1.53e-70

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 211.77  E-value: 1.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099    6 ETIDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLARMHSQFWRFWTQIEIHPGAQIDSGVFIDHGSGL 85
Cdd:TIGR01172   3 EDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGTGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   86 VIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAK 165
Cdd:TIGR01172  83 VIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVPAR 162
PLN02739 PLN02739
serine acetyltransferase
 8-190 9.29e-41

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 141.71  E-value: 9.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   8 IDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLA-----RMHSQFwrfwtQIEIHPGAQIDSGVFIDHG 82
Cdd:PLN02739 149 VQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLAlalqsRVSEVF-----GIDIHPAARIGKGILLDHG 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  83 SGLVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGI 162
Cdd:PLN02739 224 TGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN 303

                        170       180
                 ....*....|....*....|....*...
gi 446462099 163 PAKIVRLHGKKDEPVIHEVEEKREYYVN 190
Cdd:PLN02739 304 PAKLIGFVDEQDPSLTMEYDATREFFQN 331
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 63-163 8.57e-35

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: 118.70  E-value: 8.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  63 TQIEIHPGAQIDSGVFIDHGSGLVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAK 142
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 446462099 143 VGAAAVVVADVPSDVTVVGIP 163
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 6-173 2.19e-76

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: 226.89  E-value: 2.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   6 ETIDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLARMHSQFWRFWTQIEIHPGAQIDSGVFIDHGSGL 85
Cdd:COG1045    7 EDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  86 VIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAK 165
Cdd:COG1045   87 VIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPAR 166


                 ....*...
gi 446462099 166 IVRLHGKK 173
Cdd:COG1045  167 IVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 6-165 1.53e-70

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 211.77  E-value: 1.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099    6 ETIDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLARMHSQFWRFWTQIEIHPGAQIDSGVFIDHGSGL 85
Cdd:TIGR01172   3 EDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGTGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   86 VIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAK 165
Cdd:TIGR01172  83 VIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVPAR 162
PLN02739 PLN02739
serine acetyltransferase
 8-190 9.29e-41

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 141.71  E-value: 9.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   8 IDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLA-----RMHSQFwrfwtQIEIHPGAQIDSGVFIDHG 82
Cdd:PLN02739 149 VQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLAlalqsRVSEVF-----GIDIHPAARIGKGILLDHG 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  83 SGLVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGI 162
Cdd:PLN02739 224 TGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN 303

                        170       180
                 ....*....|....*....|....*...
gi 446462099 163 PAKIVRLHGKKDEPVIHEVEEKREYYVN 190
Cdd:PLN02739 304 PAKLIGFVDEQDPSLTMEYDATREFFQN 331
cysE PRK11132
serine acetyltransferase; Provisional
 8-167 3.10e-40

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 137.91  E-value: 3.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   8 IDIVKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLA-----RMHSQFwrfwtQIEIHPGAQIDSGVFIDHG 82
Cdd:PRK11132  85 IQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAiylqnQISVAF-----QVDIHPAAKIGRGIMLDHA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  83 SGLVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGI 162
Cdd:PRK11132 160 TGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGV 239


                 ....*
gi 446462099 163 PAKIV 167
Cdd:PRK11132 240 PARIV 244
PLN02694 PLN02694
serine O-acetyltransferase
 15-180 1.45e-39

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 137.08  E-value: 1.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  15 DPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLA-RMHSQFWRFWTqIEIHPGAQIDSGVFIDHGSGLVIGETAIV 93
Cdd:PLN02694 111 DPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLAlALHSRISDVFA-VDIHPAAKIGKGILFDHATGVVIGETAVI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  94 EKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAKIVrlhGKK 173
Cdd:PLN02694 190 GNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV---GGK 266


                 ....*..
gi 446462099 174 DEPVIHE 180
Cdd:PLN02694 267 EKPAKHE 273
PLN02357 PLN02357
serine acetyltransferase
 11-180 8.92e-38

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 133.85  E-value: 8.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  11 VKENDPAARTTLEVLLTYPGVKALAAHRLSHFLWKYDFKLLA-----RMHSQFwrfwtQIEIHPGAQIDSGVFIDHGSGL 85
Cdd:PLN02357 173 VKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILAlliqnRVSEAF-----AVDIHPGAKIGQGILLDHATGV 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  86 VIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAk 165
Cdd:PLN02357 248 VIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPA- 326

                        170
                 ....*....|....*
gi 446462099 166 ivRLHGKKDEPVIHE 180
Cdd:PLN02357 327 --RLIGGKENPIKHD 339
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 63-163 8.57e-35

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: 118.70  E-value: 8.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  63 TQIEIHPGAQIDSGVFIDHGSGLVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGENAK 142
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 446462099 143 VGAAAVVVADVPSDVTVVGIP 163
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 71-140 8.77e-10

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: 53.02  E-value: 8.77e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  71 AQIDSGVFIDHGSglVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGEN 140
Cdd:cd00208    1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDN 68
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 72-168 5.39e-06

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: 44.03  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  72 QIDSGVFIDHGSglVIGETAIVEKGVLLYHGVTLG------------------GTGKDCGK-RHPTVRKGALISAHAQVI 132
Cdd:cd03358    6 IIGTNVFIENDV--KIGDNVKIQSNVSIYEGVTIEddvfigpnvvftndlyprSKIYRKWElKGTTVKRGASIGANATIL 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446462099 133 GPVEIGENAKVGAAAVVVADVPSDVTVVGIPAKIVR 168
Cdd:cd03358   84 PGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10191 PRK10191
putative acyl transferase; Provisional
 34-166 2.33e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 42.57  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  34 LAAHRLSHF--LWKYDF---KLLARMHSQFWRFWTQI----EIHPGAQIDSGVFIDHGSGLVIGETAIVEKGVLLYHGVT 104
Cdd:PRK10191   2 VLAYRVAHFcsVWRKKNvlnNLWAAPLLVLYRIITECffgyEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446462099 105 LGGTGKD---CgkrhPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPAKI 166
Cdd:PRK10191  82 IGNRGADnmaC----PHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 49-164 5.21e-05

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: 42.48  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099   49 KLLARMHSQFWRFWTQIeiHPGAQIDSGVFIDHGS----------GLVIGETAIVEKGVLLYH------------GVTLG 106
Cdd:TIGR03570  74 RLVEKLKAKGYRFATLI--HPSAIVSPSASIGEGTvimagavinpDVRIGDNVIINTGAIVEHdcvigdfvhiapGVTLS 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446462099  107 GtgkdcgkrHPTVRKGALISAHAQVIGPVEIGENAKVGAAAVVVADVPSDVTVVGIPA 164
Cdd:TIGR03570 152 G--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 49-140 8.49e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.31  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  49 KLLARMHSQFwRFWTQIE----IHPGAQIDSGVFIDHGSglVIGETAIVEKGVLLYHGVTLggtGKDCgkrhpTVRKGAL 124
Cdd:COG1044   84 KLLQLFYPPP-APAPGIHpsavIDPSAKIGEGVSIGPFA--VIGAGVVIGDGVVIGPGVVI---GDGV-----VIGDDCV 152

                         90
                 ....*....|....*..
gi 446462099 125 ISAHAqVIGP-VEIGEN 140
Cdd:COG1044  153 LHPNV-TIYErCVIGDR 168
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
52-168 2.62e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 39.47  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  52 ARMHSQFWRFWTQIEIHPGAQIDSGVFIDHGSGLVIGETAIVEKGVLLY---HGVTLGGTGKDCGKrHPTVRKGALISAH 128
Cdd:COG0110   15 VVIGPGVRIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILtgnHPIDDPATFPLRTG-PVTIGDDVWIGAG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446462099 129 AQVIGPVEIGENakvgaaavvvadvPSDVTVVGIPAKIVR 168
Cdd:COG0110   94 ATILPGVTIGDGavvgagsvvtkdvPPYAIVAGNPARVIR 133
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 66-106 4.71e-04

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: 39.70  E-value: 4.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446462099  66 EIHPGAQIDSGVFIDHGSglVIGETAIVEKGVLLYHGVTLG 106
Cdd:cd03352   21 VIGDGVVIGPGVVIGDGV--VIGDDCVIHPNVTIYEGCIIG 59
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 49-140 1.47e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  49 KLLARMHSQFWRFwTQIEIHPGAQIDSGVfidhgsglVIGETAIVEKGVLLYHGVTLGgtgkdcgkrhptvrKGALISAH 128
Cdd:PRK00892  86 RLAQLFDPPATPS-PAAGIHPSAVIDPSA--------KIGEGVSIGPNAVIGAGVVIG--------------DGVVIGAG 142

                         90
                 ....*....|...
gi 446462099 129 AqVIGP-VEIGEN 140
Cdd:PRK00892 143 A-VIGDgVKIGAD 154
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 70-140 2.70e-03

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 36.59  E-value: 2.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446462099  70 GAQIDSGVFIDhgSGLVIGETAIVEKGVLLYHGVTLGGTGKDCGKRHPTVRKGALISAHAQVIGPVEIGEN 140
Cdd:cd03350   31 GAYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKG 99
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 62-168 4.16e-03

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 36.19  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446462099  62 WTQIEIHPGAQIDSGVFIdHGsglVIGETAIVEKGVLLYHGVTLGGTgkdcgkrhpTVRKGALISAHAQVIGPVEIGENA 141
Cdd:cd04745   37 FGRIVIRDGANVQDNCVI-HG---FPGQDTVLEENGHIGHGAILHGC---------TIGRNALVGMNAVVMDGAVIGEES 103

                         90       100
                 ....*....|....*....|....*....
gi 446462099 142 KVGAAA--VVVADVPSDVTVVGIPAKIVR 168
Cdd:cd04745  104 IVGAMAfvKAGTVIPPRSLIAGSPAKVIR 132
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
67-140 9.40e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 35.84  E-value: 9.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446462099  67 IHPGAQIDSGVFIdhGSGLVIGETAIVEKGVLLYHGVTLGgtgkdcgkrhptvrkgalisAHAQVIGPVEIGEN 140
Cdd:PRK05289   5 IHPTAIVEPGAKI--GENVEIGPFCVIGPNVVIGDGTVIG--------------------SHVVIDGHTTIGKN 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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