NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|323516145|gb|ADX90526|]
View 

hypothetical protein ABTW07_0087 [Acinetobacter baumannii TCDC-AB0715]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 3-207 9.38e-51

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


The actual alignment was detected with superfamily member TIGR03570:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 201  Bit Score: 163.05  E-value: 9.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145    3 KLAIIGSGGFAKELLDLAIDQGYHQICFL-ERNAKDGDALLGFPILA--ESVIPTLTDTVYA-IGVADPKNRKRIYETY- 77
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADILERSGWEVVGFLdDNPALQGTEVDGLPVLGgdEDLLRYPPDEVDLvVAIGDNKLRRRLVEKLk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145   78 -PDLTYPNLIHSQASLGYGIRelLEdsKGIVIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANISGCVHL 156
Cdd:TIGR03570  81 aKGYRFATLIHPSAIVSPSAS--IG--EGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 323516145  157 MQGTYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPA 207
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVT------IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 3-207 9.38e-51

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: 163.05  E-value: 9.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145    3 KLAIIGSGGFAKELLDLAIDQGYHQICFL-ERNAKDGDALLGFPILA--ESVIPTLTDTVYA-IGVADPKNRKRIYETY- 77
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADILERSGWEVVGFLdDNPALQGTEVDGLPVLGgdEDLLRYPPDEVDLvVAIGDNKLRRRLVEKLk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145   78 -PDLTYPNLIHSQASLGYGIRelLEdsKGIVIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANISGCVHL 156
Cdd:TIGR03570  81 aKGYRFATLIHPSAIVSPSAS--IG--EGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 323516145  157 MQGTYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPA 207
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVT------IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-206 4.21e-47

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: 153.79  E-value: 4.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145   6 IIGSGGFAKELLDLAIDQGYHQIC-FLERNAKDGDALLGFPILAESVIPTLT---DTVYAIGVADPKNRKRIYETY--PD 79
Cdd:cd03360    1 IIGAGGHARVVADILEADSGYEVVgFLDDDPELKGTEGLGLPVGLDELLLLYpppDDEFVVAIGDNKLRRKLAEKLlaAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145  80 LTYPNLIHSQASLGYGIRelLEdsKGIVIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANISGCVHLMQG 159
Cdd:cd03360   81 YRFATLIHPSAVVSPSAV--IG--EGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 323516145 160 TYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSP 206
Cdd:cd03360  157 AFIGAGATIIQGVT------IGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
104-212 9.05e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 71.06  E-value: 9.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 104 KGIVIAAGARITNS-CRFGNFIIVSFNSTI--GHDCILENYVSIMPGANISGCVHLMQ----------------GTYVGT 164
Cdd:COG0110   13 DGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDdpatfplrtgpvtigdDVWIGA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 323516145 165 NVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELRR 212
Cdd:COG0110   93 GATILPGVT------IGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
PRK10502 PRK10502
putative acyl transferase; Provisional
 104-211 4.72e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.50  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 104 KGIVIAAGARITnscrFGNFIIVSFNSTIGHDCILENYVSIMPGAN--ISGCVHLM---------------------QGT 160
Cdd:PRK10502  56 KGVVIRPSVRIT----YPWKLTIGDYAWIGDDVWLYNLGEITIGAHcvISQKSYLCtgshdysdphfdlntapivigEGC 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 323516145 161 YVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELR 211
Cdd:PRK10502 132 WLAADVFVAPGVT------IGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 3-75 8.51e-09

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 50.64  E-value: 8.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323516145    3 KLAIIGSGGFAKELLDLAIDQG-YHQICFLERNAKDGdaLLGFPILAESV--IPTLTDTVYAIGVA--DPKNRKRIYE 75
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAMGeYEIIGFLDDNKKTE--VNGYPVLGGDIdlLASLSPDEYDVVIAigNNKVRKKIAE 76
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 3-207 9.38e-51

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: 163.05  E-value: 9.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145    3 KLAIIGSGGFAKELLDLAIDQGYHQICFL-ERNAKDGDALLGFPILA--ESVIPTLTDTVYA-IGVADPKNRKRIYETY- 77
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADILERSGWEVVGFLdDNPALQGTEVDGLPVLGgdEDLLRYPPDEVDLvVAIGDNKLRRRLVEKLk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145   78 -PDLTYPNLIHSQASLGYGIRelLEdsKGIVIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANISGCVHL 156
Cdd:TIGR03570  81 aKGYRFATLIHPSAIVSPSAS--IG--EGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 323516145  157 MQGTYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPA 207
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVT------IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-206 4.21e-47

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: 153.79  E-value: 4.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145   6 IIGSGGFAKELLDLAIDQGYHQIC-FLERNAKDGDALLGFPILAESVIPTLT---DTVYAIGVADPKNRKRIYETY--PD 79
Cdd:cd03360    1 IIGAGGHARVVADILEADSGYEVVgFLDDDPELKGTEGLGLPVGLDELLLLYpppDDEFVVAIGDNKLRRKLAEKLlaAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145  80 LTYPNLIHSQASLGYGIRelLEdsKGIVIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANISGCVHLMQG 159
Cdd:cd03360   81 YRFATLIHPSAVVSPSAV--IG--EGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 323516145 160 TYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSP 206
Cdd:cd03360  157 AFIGAGATIIQGVT------IGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
104-212 9.05e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 71.06  E-value: 9.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 104 KGIVIAAGARITNS-CRFGNFIIVSFNSTI--GHDCILENYVSIMPGANISGCVHLMQ----------------GTYVGT 164
Cdd:COG0110   13 DGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDdpatfplrtgpvtigdDVWIGA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 323516145 165 NVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELRR 212
Cdd:COG0110   93 GATILPGVT------IGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 104-211 1.59e-13

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: 64.44  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 104 KGIVIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGA-----NISGC----------VHLMQGTYVGTNVAV 168
Cdd:cd03358    3 DNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVvftndLYPRSkiyrkwelkgTTVKRGASIGANATI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 323516145 169 LPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELR 211
Cdd:cd03358   83 LPGVT------IGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 129-211 2.70e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.96  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 129 NSTI----GHDCILENYVSIMPGANISGCvHLMQGTYVGTNVAVLPGknpellkC-LGENSVIGAGAVVV--KHTEPNKV 201
Cdd:COG0663   61 GVVLhvdpGYPLTIGDDVTIGHGAILHGC-TIGDNVLIGMGAIVLDG-------AvIGDGSIVGAGALVTegKVVPPGSL 132

                         90
                 ....*....|
gi 323516145 202 YIGSPAKELR 211
Cdd:COG0663  133 VVGSPAKVVR 142
PRK10502 PRK10502
putative acyl transferase; Provisional
 104-211 4.72e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.50  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 104 KGIVIAAGARITnscrFGNFIIVSFNSTIGHDCILENYVSIMPGAN--ISGCVHLM---------------------QGT 160
Cdd:PRK10502  56 KGVVIRPSVRIT----YPWKLTIGDYAWIGDDVWLYNLGEITIGAHcvISQKSYLCtgshdysdphfdlntapivigEGC 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 323516145 161 YVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELR 211
Cdd:PRK10502 132 WLAADVFVAPGVT------IGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 102-212 1.63e-09

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: 54.68  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 102 DSKGIVIAAGARITNSCrfgnfIIVSFNstiGHDCILENYVSIMPGANISGCvHLMQGTYVGTNVAVLPGKNpellkcLG 181
Cdd:cd04745   36 DFGRIVIRDGANVQDNC-----VIHGFP---GQDTVLEENGHIGHGAILHGC-TIGRNALVGMNAVVMDGAV------IG 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 323516145 182 ENSVIGAGAVVVK--HTEPNKVYIGSPAKELRR 212
Cdd:cd04745  101 EESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRE 133
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 124-208 1.70e-09

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: 53.23  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 124 IIVSFNSTIGHDCIL--------ENYVSIMPGANISGCVHLMQ-------------------GTYVGTNVAVLPGKnpel 176
Cdd:cd04647    2 ISIGDNVYIGPGCVIsagggitiGDNVLIGPNVTIYDHNHDIDdperpieqgvtsapivigdDVWIGANVVILPGV---- 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 323516145 177 lkCLGENSVIGAGAVVVKHTEPNKVYIGSPAK 208
Cdd:cd04647   78 --TIGDGAVVGAGSVVTKDVPPNSIVAGNPAK 107
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 129-211 2.24e-09

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: 53.95  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 129 NSTI----GHDCILENYVSIMPGANISGCvHLMQGTYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHT--EPNKVY 202
Cdd:cd04645   50 GSVLhvdpGYPTIIGDNVTVGHGAVLHGC-TIGDNCLIGMGAIILDGAV------IGKGSIVAAGSLVPPGKviPPGSLV 122


                 ....*....
gi 323516145 203 IGSPAKELR 211
Cdd:cd04645  123 AGSPAKVVR 131
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 131-208 7.08e-09

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 51.84  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 131 TIGHDCILENYVSIMPGAN---------ISGCVHLMQGTYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKV 201
Cdd:cd05825   25 TIGSDACISQGAYLCTGSHdyrspafplITAPIVIGDGAWVAAEAFVGPGVT------IGEGAVVGARSVVVRDLPAWTV 98


                 ....*..
gi 323516145 202 YIGSPAK 208
Cdd:cd05825   99 YAGNPAV 105
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 3-75 8.51e-09

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 50.64  E-value: 8.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323516145    3 KLAIIGSGGFAKELLDLAIDQG-YHQICFLERNAKDGdaLLGFPILAESV--IPTLTDTVYAIGVA--DPKNRKRIYE 75
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAMGeYEIIGFLDDNKKTE--VNGYPVLGGDIdlLASLSPDEYDVVIAigNNKVRKKIAE 76
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 105-206 6.68e-08

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: 48.98  E-value: 6.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 105 GIVIAAGARITNSCRFGNF--IIVSFNSTIGHDCILENYVSIMPGANIS--GCVHLMQGTYVGTNVAVLpGKNpellkCL 180
Cdd:cd03354    2 GIDIHPGAKIGPGLFIDHGtgIVIGETAVIGDNCTIYQGVTLGGKGKGGgkRHPTIGDNVVIGAGAKIL-GNI-----TI 75

                         90       100
                 ....*....|....*....|....*.
gi 323516145 181 GENSVIGAGAVVVKHTEPNKVYIGSP 206
Cdd:cd03354   76 GDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 107-212 2.09e-07

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: 49.33  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 107 VIAAGARITNSCrfgnfiivsfnsTIGHDCILENYVSIMPGANISGCVHLMQGTYVGTNVAVLPGKNpellkcLGENSVI 186
Cdd:cd03352  116 VIGDGTKIDNLV------------QIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLT------IGDGVVI 177

                         90       100
                 ....*....|....*....|....*.
gi 323516145 187 GAGAVVVKHTEPNKVYIGSPAKELRR 212
Cdd:cd03352  178 GAGSGVTSIVPPGEYVSGTPAQPHRE 203
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 162-208 2.93e-07

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: 48.57  E-value: 2.93e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 323516145 162 VGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAK 208
Cdd:cd03357  127 IGGGVIILPGVT------IGDNSVIGAGSVVTKDIPANVVAAGNPAR 167
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 120-212 2.96e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 49.23  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 120 FGNF---IIVSFNSTIGHDCILENYVSI------------MPGANISGCVHLMQGTYVGTNVAVLPGKNpellkcLGENS 184
Cdd:PRK09527  83 YANFnltIVDDYTVTIGDNVLIAPNVTLsvtghpvhhelrKNGEMYSFPITIGNNVWIGSHVVINPGVT------IGDNS 156

                         90       100
                 ....*....|....*....|....*...
gi 323516145 185 VIGAGAVVVKHTEPNKVYIGSPAKELRR 212
Cdd:PRK09527 157 VIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 96-212 2.96e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 42.88  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145  96 IRELLEDSKGIVIAAGARitnsCRFGNFIIVSFNSTIGHDCILENYVSIMPGAN--ISGCVHLMQGTY------------ 161
Cdd:PRK10092  50 LADLFGQVTEAYIEPTFR----CDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNcmLAPGVHIYTATHpldpvarnsgae 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323516145 162 ------VGTNV-----AVLpgkNPELlkCLGENSVIGAGAVVVKHTEPNKVYIGSPAKELRR 212
Cdd:PRK10092 126 lgkpvtIGNNVwiggrAVI---NPGV--TIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 162-211 4.99e-05

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: 41.76  E-value: 4.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 323516145 162 VGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELR 211
Cdd:cd03349   82 IGHGATILPGVT------IGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 105-213 6.90e-05

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: 41.99  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 105 GIVIAAGARItnSCRFgnFI-----IVsfnstIGHDCILENYVSIMPGANISGC--------VHLMQGTYVGTNVAVLPG 171
Cdd:COG1045   65 GIDIHPGATI--GRGF--FIdhgtgVV-----IGETAVIGDNVTIYQGVTLGGTgkekgkrhPTIGDNVVIGAGAKILGP 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 323516145 172 KNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELRRD 213
Cdd:COG1045  136 IT------IGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRK 171
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 151-211 2.44e-04

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 40.63  E-value: 2.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323516145 151 SGCVHLMQGTYVGTNVAVLPGKNpellkcLGENSVIGAGAVVVKHTEPNKVYIGSPAKELR 211
Cdd:PRK09677 128 SSAVVIGQRVWIGENVTILPGVS------IGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 26-192 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 323516145  26 HQICFLErNAKDGDALL----GFPILAESVIPTLTDTVYAIGVADPknrkriYETYPDLT---YPNLIHSQASlgyGIre 98
Cdd:PRK00892  36 GQISFLA-NPKYRKQLAttkaGAVIVSPDDAEFVPAGNALLVVKNP------YLAFARLAqlfDPPATPSPAA---GI-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145  99 lledSKGIVIAAGARITNSCRFGNfiivsfNSTIGHDCILENYVSIMPGANISGCVHLMQGTYVGTNVAVLPGknpellk 178
Cdd:PRK00892 104 ----HPSAVIDPSAKIGEGVSIGP------NAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA------- 166

                        170
                 ....*....|....*
gi 323516145 179 C-LGENSVIGAGAVV 192
Cdd:PRK00892 167 VrIGNRVIIHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 107-154 1.49e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.16  E-value: 1.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 323516145 107 VIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANI-------SGCV 154
Cdd:cd03352   15 VIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIgdrviihSGAV 69
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 126-212 5.35e-03

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: 36.01  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 126 VSFNSTIGHDCILENYVSIMPGAnisgcvhLMQGTYVGTNVAVlpGKNPELLKC--LGENSVIGAGAVVVKHTE--PNKV 201
Cdd:cd04650   52 VSIHTDHGYPTEIGDYVTIGHNA-------VVHGAKVGNYVIV--GMGAILLNGakIGDHVIIGAGAVVTPGKEipDYSL 122

                         90
                 ....*....|.
gi 323516145 202 YIGSPAKELRR 212
Cdd:cd04650  123 VLGVPAKVVRK 133
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 126-192 7.22e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 34.15  E-value: 7.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323516145 126 VSFNSTIGHDCILENYVSIMPGANISGCVHLMQ--GTYVGTNVAVlpGKNPELLKC--LGENSVIGAGAVV 192
Cdd:cd00208    9 IHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEknPTIIGDNVEI--GANAVIHGGvkIGDNAVIGAGAVV 77
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 107-201 8.47e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.15  E-value: 8.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323516145 107 VIAAGARITNSCRFGNFIIVSFNSTIGHDCILENYVSIMPGANISGCVHLMQGTYVGTNVAVLPGKNPELLKCLGENSVI 186
Cdd:PRK12461   7 VIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGEESRLEIGDRNVI 86

                         90
                 ....*....|....*
gi 323516145 187 GAGAVVVKHTEPNKV 201
Cdd:PRK12461  87 REGVTIHRGTKGGGV 101
 
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