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Conserved domains on  [gi|15598323|ref|NP_251817|]
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hypothetical protein PA3127 [Pseudomonas aeruginosa PAO1]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 19004847)

GNAT family N-acetyltransferase which catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; contains a N-terminal vicinal oxygen chelate (VOC) domain which uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms, and which is similar to bleomycin binding protein (BMLA) which binds bleomycin

EC:  2.3.1.-
PubMed:  10940244

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 5-115 6.75e-46

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


:

Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 149.68  E-value: 6.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   5 IPTFPCRDLDSASAFY-QSLGFHLGARY--PTYAILQRGALELHLSLFEALEPKTNCSAAYLRLEDAQALHRQAAALGLG 81
Cdd:cd08349   1 IPILPVRDIDKTLAFYvDVLGFEVDYERppPGYAILSRGGVELHLFEHPGLDPAGSGVAAYIRVEDIDALHAELKAAGLP 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598323  82 SQGIPRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd08349  81 LFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
125-257 1.02e-14

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.02  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323 125 RVRLASADDVPAVAALWQANVREAGET--LDAGDQQAIQALLLAASRNRLLWL-AEAQQHPRGFVLAHLWQIEDGQARVG 201
Cdd:COG1247   3 TIRPATPEDAPAIAAIYNEAIAEGTATfeTEPPSEEEREAWFAAILAPGRPVLvAEEDGEVVGFASLGPFRPRPAYRGTA 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598323 202 EIAeLYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGW 257
Cdd:COG1247  83 EES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 5-115 6.75e-46

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 149.68  E-value: 6.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   5 IPTFPCRDLDSASAFY-QSLGFHLGARY--PTYAILQRGALELHLSLFEALEPKTNCSAAYLRLEDAQALHRQAAALGLG 81
Cdd:cd08349   1 IPILPVRDIDKTLAFYvDVLGFEVDYERppPGYAILSRGGVELHLFEHPGLDPAGSGVAAYIRVEDIDALHAELKAAGLP 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598323  82 SQGIPRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd08349  81 LFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
3-116 2.59e-16

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 72.97  E-value: 2.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   3 RAIPTFPCRDLDSASAFYQS-LGFHLGARYPT------YAILQRGALELHLSLFEALEPKT--NCSAAYLRLEDAQALHR 73
Cdd:COG2764   1 SVTPYLVVDDAEEALEFYEDvFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPPDSPAAegNGVSLSLYVDDVDALFA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598323  74 QAAAlglgsQGIPRITALEDQPWGMREFALVDPDGNLLRVGQE 116
Cdd:COG2764  81 RLVA-----AGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
125-257 1.02e-14

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.02  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323 125 RVRLASADDVPAVAALWQANVREAGET--LDAGDQQAIQALLLAASRNRLLWL-AEAQQHPRGFVLAHLWQIEDGQARVG 201
Cdd:COG1247   3 TIRPATPEDAPAIAAIYNEAIAEGTATfeTEPPSEEEREAWFAAILAPGRPVLvAEEDGEVVGFASLGPFRPRPAYRGTA 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598323 202 EIAeLYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGW 257
Cdd:COG1247  83 EES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 173-238 4.88e-08

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 48.81  E-value: 4.88e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598323 173 LWLAEAQQHPRGFVLAHlwqIEDGQARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIR 238
Cdd:cd04301   1 FLVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 170-257 1.05e-07

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 49.44  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   170 NRLLWLAEAQQHPRGFVLAHlwqIEDGQARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSN 249
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLS---IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAI 108


                  ....*...
gi 15598323   250 LFWQGLGW 257
Cdd:pfam00583 109 ALYEKLGF 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-113 8.69e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 43.98  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323     7 TFPCRDLDSASAFYQS-LGFHLGARYP-------TYAILQRGALELHLSLFEALEPKTN------CSAAYLRLEDAQALH 72
Cdd:pfam00903   6 ALRVGDLEKSLDFYTDvLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAgfgghhIAFIAFSVDDVDAAY 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15598323    73 RQAAAlglgsQGIPRITALEDQPWGMREFALVDPDGNLLRV 113
Cdd:pfam00903  86 DRLKA-----AGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
PRK03624 PRK03624
putative acetyltransferase; Provisional
 126-260 4.18e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323  126 VRLASADDVPAVAALWQAnvreAGETLDAGDQQAIQALLLAASrNRLLWLAEAQQHPRGFVLAHLwqieDGQArvGEIAE 205
Cdd:PRK03624   5 IRVFRQADFEAVIALWER----CDLTRPWNDPEMDIERKLNHD-PSLFLVAEVGGEVVGTVMGGY----DGHR--GWAYY 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15598323  206 LYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGWDAD 260
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 5-115 6.75e-46

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 149.68  E-value: 6.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   5 IPTFPCRDLDSASAFY-QSLGFHLGARY--PTYAILQRGALELHLSLFEALEPKTNCSAAYLRLEDAQALHRQAAALGLG 81
Cdd:cd08349   1 IPILPVRDIDKTLAFYvDVLGFEVDYERppPGYAILSRGGVELHLFEHPGLDPAGSGVAAYIRVEDIDALHAELKAAGLP 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598323  82 SQGIPRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd08349  81 LFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
BLMT_like cd08350
BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT ...
 1-116 7.63e-33

BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMT has strong binding affinity to Bm and it protects against this lethal compound through drug sequestering. BLMT has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMT is a dimer with two Bm-binding pockets formed at the dimer interface.


Pssm-ID: 319938  Cd Length: 118  Bit Score: 116.22  E-value: 7.63e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   1 MERAIPTFPCRDLDSASAFYQSLGFHLGARYPTYAILQRGALELHLSLFEALEPKTNCSAAYLRLEDAQALHRQAAALGL 80
Cdd:cd08350   1 TDRATPNLPSRDFDATAAFYARLGFQTVYRDDGWMILRRGDLTLEFFPHPDLDPAASWFSCCLRVDDLDALYAQWSAAGI 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598323  81 --GSQGIPRITALEDQPWGMREFALVDPDGNLLRVGQE 116
Cdd:cd08350  81 peDTRGIPRLHPPQTQPWGIRMFALIDPDGSLLRLIQN 118
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 4-115 1.24e-20

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The VOC superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319944  Cd Length: 113  Bit Score: 84.28  E-value: 1.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   4 AIPTF-PCRDLDSASAFYQSLGFHLGARYPTYAILQRGALELHLSLFEALEPKTNCsAAYLRLEDAQALHRQAAALGLGS 82
Cdd:cd08356   2 EIKAFvPAKDFELSKAFYQALGFELASEEGGVAYFRLGDCSFLLQDFYEKEHAENF-MMHLLVEDVDAWHQHVKTLGLAE 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15598323  83 QGIPRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd08356  81 RYGVKVTDPTDQPWGMRDFVLTDPSGVLWRIGQ 113
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
3-116 2.59e-16

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 72.97  E-value: 2.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   3 RAIPTFPCRDLDSASAFYQS-LGFHLGARYPT------YAILQRGALELHLSLFEALEPKT--NCSAAYLRLEDAQALHR 73
Cdd:COG2764   1 SVTPYLVVDDAEEALEFYEDvFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPPDSPAAegNGVSLSLYVDDVDALFA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598323  74 QAAAlglgsQGIPRITALEDQPWGMREFALVDPDGNLLRVGQE 116
Cdd:COG2764  81 RLVA-----AGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
125-257 1.02e-14

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.02  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323 125 RVRLASADDVPAVAALWQANVREAGET--LDAGDQQAIQALLLAASRNRLLWL-AEAQQHPRGFVLAHLWQIEDGQARVG 201
Cdd:COG1247   3 TIRPATPEDAPAIAAIYNEAIAEGTATfeTEPPSEEEREAWFAAILAPGRPVLvAEEDGEVVGFASLGPFRPRPAYRGTA 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598323 202 EIAeLYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGW 257
Cdd:COG1247  83 EES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
126-257 2.97e-12

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.80  E-value: 2.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323 126 VRLASADDVPAVAALWQanvreagETLDAGDQQAIQALLLAASRNRLLWLAEAQQHPRGFVLAHLWQIeDGQARVGEIAE 205
Cdd:COG3153   1 IRPATPEDAEAIAALLR-------AAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDI-DGEGPALLLGP 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15598323 206 LYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSaldAPLSNLFWQGLGW 257
Cdd:COG3153  73 LAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGF 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-113 1.47e-11

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 59.85  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   7 TFPCRDLDSASAFYQS-LGFHLGARY--PTYAILQRGAlELHLSLFEALEPKTNCSAAY----LRLEDAQALHRQAAALG 79
Cdd:cd06587   3 ALRVPDLDASVAFYEEvLGFEVVSRNegGGFAFLRLGP-GLRLALLEGPEPERPGGGGLfhlaFEVDDVDEVDERLREAG 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598323  80 lgsQGIPRITALEDQPWGMREFALVDPDGNLLRV 113
Cdd:cd06587  82 ---AEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-118 2.41e-09

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 53.87  E-value: 2.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   1 MERAIPTFPCRDLDSASAFYQS-LGFHLGARYP---TYAILQRGA-LELHLSLFEAlEPKTNCSAAYLRLEDAQALHRQA 75
Cdd:COG3324   3 GTIVWVELPVDDLERAKAFYEEvFGWTFEDDAGpggDYAEFDTDGgQVGGLMPGAE-EPGGPGWLLYFAVDDLDAAVARV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598323  76 AALGlgsqgIPRITALEDQPWGMREFALVDPDGNLLRVGQELD 118
Cdd:COG3324  82 EAAG-----GTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQPAA 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-119 5.60e-09

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 53.07  E-value: 5.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   7 TFPCRDLDSASAFYQS-LGFHLGARYP------TYAILQRG-ALELHLSLFEALEPKTNCSAA---YLRLEDAQALHRQA 75
Cdd:COG0346   7 TLRVSDLEASLAFYTDvLGLELVKRTDfgdggfGHAFLRLGdGTELELFEAPGAAPAPGGGGLhhlAFRVDDLDAAYARL 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15598323  76 AALGLGSQGIPRitaleDQPWGMREFALVDPDGNLLRVGQELDA 119
Cdd:COG0346  87 RAAGVEIEGEPR-----DRAYGYRSAYFRDPDGNLIELVEPPPG 125
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 125-246 2.01e-08

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 51.53  E-value: 2.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323 125 RVRLASADDVPAVAALwqanvreagetldagdqqaIQALLLAASRNRLlWLAEAQQHPRGFVlahlwQIEDGQARVGEIA 204
Cdd:COG1246   2 TIRPATPDDVPAILEL-------------------IRPYALEEEIGEF-WVAEEDGEIVGCA-----ALHPLDEDLAELR 56

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15598323 205 ELYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAP 246
Cdd:COG1246  57 SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAI 98
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 184-257 4.14e-08

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 49.65  E-value: 4.14e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598323 184 GFVLAHLwqieDGQARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGW 257
Cdd:COG0456   1 GFALLGL----VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGF 70
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 173-238 4.88e-08

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 48.81  E-value: 4.88e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598323 173 LWLAEAQQHPRGFVLAHlwqIEDGQARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIR 238
Cdd:cd04301   1 FLVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 170-257 1.05e-07

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 49.44  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   170 NRLLWLAEAQQHPRGFVLAHlwqIEDGQARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSN 249
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLS---IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAI 108


                  ....*...
gi 15598323   250 LFWQGLGW 257
Cdd:pfam00583 109 ALYEKLGF 116
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 65-115 1.54e-07

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319962  Cd Length: 121  Bit Score: 49.03  E-value: 1.54e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15598323  65 LEDAQALHRQAAAlglgsQGIPRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd16355  76 VDDVDALHRECRA-----RGADIRQPPTDMPWGMREMHVRHPDGHRFRVGQ 121
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-115 6.18e-07

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 47.39  E-value: 6.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   3 RAIPTFPCRDLDSASAFYQSlgfHLGARYPT----YAILQRG---ALEL------HLSLFEALEPKTNCSAAYLRLEDAQ 69
Cdd:cd08359   2 SLGPVIVTEDVAATAAFYVK---HFGFRVIFdsdwYVSLRRAerhGFELaimdgqHGAVPAASQTQSSGLIINFEVDDAD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15598323  70 ALHRQaaalgLGSQGIPRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd08359  79 AEYER-----LTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLIDVIQ 119
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 169-245 1.15e-06

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 45.52  E-value: 1.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598323   169 RNRLLWLAEAQQHPRGFVLAHlwqIEDGQARVGEIAeLYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDA 245
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALL---PLDDEGALAELR-LAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRA 73
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-113 8.69e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 43.98  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323     7 TFPCRDLDSASAFYQS-LGFHLGARYP-------TYAILQRGALELHLSLFEALEPKTN------CSAAYLRLEDAQALH 72
Cdd:pfam00903   6 ALRVGDLEKSLDFYTDvLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAgfgghhIAFIAFSVDDVDAAY 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15598323    73 RQAAAlglgsQGIPRITALEDQPWGMREFALVDPDGNLLRV 113
Cdd:pfam00903  86 DRLKA-----AGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
Glyoxalase_7 pfam19581
Glyoxalase superfamily protein;
2-118 1.61e-05

Glyoxalase superfamily protein;


Pssm-ID: 437413  Cd Length: 133  Bit Score: 43.44  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323     2 ERAIPTFPCRDLDSASAFYQS-LGF------HLGARYPTYAILQRGALELHLSlfEALEPKTNCSAAYLRLEDAQALHRQ 74
Cdd:pfam19581  14 EQIFPILRIFDEAKAKAFYGDfLGFeadwehHFDDHFPAYIQVSRAGLGLHLS--EHHGDACPGSNIFVTMRGIDAFHKE 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15598323    75 AaalgLGSQGIPRITALEDQPWGMREFALVDPDGNLLRVGQELD 118
Cdd:pfam19581  92 I----TGKKYKFLNPGIEELFWGADCMEVIDPFGNHIRFCEQKD 131
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 58-115 4.99e-05

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319943  Cd Length: 123  Bit Score: 42.02  E-value: 4.99e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598323  58 CSAAYLRLEDAQALHRQAAALGLGSQGIPRitaleDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd08355  70 TQSVYVAVADPDAHYERARAAGAEIVMEPT-----DTDYGSRDYSARDPEGHLWSFGT 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
7-111 6.26e-05

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 41.87  E-value: 6.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   7 TFPCRDLDSASAFYQS-LGFHLGARYPTYAILQRGALELHLSLFEALEPKTNCSAAYL-----RLEDAQALhrQAAALGL 80
Cdd:COG2514   8 TLRVRDLERSAAFYTDvLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAPPRPGAAGLdhvafRVPSRADL--DAALARL 85

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598323  81 GSQGIPrITALEDqPWGMREFALVDPDGNLL 111
Cdd:COG2514  86 AAAGVP-VEGAVD-HGVGESLYFRDPDGNLI 114
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 8-109 1.18e-04

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 40.71  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   8 FPCRDLDSASAFYQSL-GFHL---GARYPTYAILQRGAlELHLSLFEALEPKT---NCSAAYLRLEDAQALHRQAAALGl 80
Cdd:cd07247   6 LPTTDLERAKAFYGAVfGWTFedeGDGGGDYALFTAGG-GAVGGLMRAPEEVAgapPGWLIYFAVDDLDAALARVEAAG- 83

                        90       100
                ....*....|....*....|....*....
gi 15598323  81 GSQGIPRItaleDQPWGMREFALVDPDGN 109
Cdd:cd07247  84 GKVVVPPT----DIPGGGRFAVFADPEGN 108
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
198-257 1.27e-04

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.89  E-value: 1.27e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323 198 ARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGW 257
Cdd:COG3393  13 PGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
188-257 1.37e-04

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.94  E-value: 1.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598323 188 AHLWQIEDGQARVGEIAelyVLPQARRQGLARELVGSAEEALRSRGAGLIRaqsaLDAPLSNL-FWQGLGW 257
Cdd:COG2153  49 ARLLPPGDGEAKIGRVA---VLPEYRGQGLGRALMEAAIEEARERGARRIV----LSAQAHAVgFYEKLGF 112
PRK03624 PRK03624
putative acetyltransferase; Provisional
 126-260 4.18e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323  126 VRLASADDVPAVAALWQAnvreAGETLDAGDQQAIQALLLAASrNRLLWLAEAQQHPRGFVLAHLwqieDGQArvGEIAE 205
Cdd:PRK03624   5 IRVFRQADFEAVIALWER----CDLTRPWNDPEMDIERKLNHD-PSLFLVAEVGGEVVGTVMGGY----DGHR--GWAYY 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15598323  206 LYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGWDAD 260
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
BAT cd16354
Bleomycin N-Acetyltransferase and similar proteins; BlmB, encodes a bleomycin ...
 4-114 9.04e-04

Bleomycin N-Acetyltransferase and similar proteins; BlmB, encodes a bleomycin N-acetyltransferase, designated BAT, which inactivates Bm using acetyl-coenzyme A (AcCoA). BAT forms a dimer structure via interaction of its C-terminal domains in the monomers. The N-terminal domain of BAT has a tunnel with two entrances: a wide entrance that accommodates the metal-binding domain of Bm and a narrow entrance that accommodates acetyl-CoA (AcCoA). A groove formed on the dimer interface of two BAT C-terminal domains forms the DNA-binding domain of Bm. In a ternary complex of BAT, BmA(2), and CoA, a thiol group of CoA is positioned near the primary amine of Bm at the midpoint of the tunnel and ensures efficient transfer of an acetyl group from AcCoA to the primary amine of Bm. BAT belongs to vicinal oxygen chelate (VOC) superfamily that is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including thiocoraline, bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319961  Cd Length: 114  Bit Score: 38.20  E-value: 9.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   4 AIPTFPCRDLDSASAFYQSLgfhLGARY-------PTYAILQRGALELHLSLFEALEPKTNCSAAYLRLE---DAQALHR 73
Cdd:cd16354   1 VEPVLPVRDVAATLDLLEAV---LGARVgfevgdpPEFAGAVLGPWSVGPGLRLVATPGGPIAPVTLHLDagvEFDSLHR 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598323  74 QAAALGLGSQGIPRitaleDQPWGMREFALVDPDGNLLRVG 114
Cdd:cd16354  78 RALAAGARVDGPPV-----RQPWGRREFVLRLPEGHRLVVS 113
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
126-266 1.07e-03

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 38.36  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323  126 VRLASADDVPAVAALwqanvreAGETLDAG-DQQAIQALLLAASRNRLL--WLAEAQQHPRGFVLAHLwQIEDGQAR-VG 201
Cdd:PRK10146   6 LRPATQYDTDAVYAL-------ICELKQAEfDHQAFRVGFNANLRDPNMryHLALLDGEVVGMIGLHL-QFHLHHVNwIG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598323  202 EIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIRAQSALDAPLSNLFWQGLGWDADYLTFTR 266
Cdd:PRK10146  78 EIQELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLREGYEQSHFRFTK 142
PRK07757 PRK07757
N-acetyltransferase;
156-233 1.25e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.25  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323  156 DQQAIQALLLAASRNRLLW---LAEAQQHPRGFVLAhlwqIEDGQ-----------ARVGEIAELYVLPQARRQGLAREL 221
Cdd:PRK07757  11 DVKAIHALINVYAKKGLMLprsLDELYENIRDFYVA----EEEGEivgccalhilwEDLAEIRSLAVSEDYRGQGIGRML 86

                         90
                 ....*....|..
gi 15598323  222 VGSAEEALRSRG 233
Cdd:PRK07757  87 VEACLEEARELG 98
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-113 1.25e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319903  Cd Length: 112  Bit Score: 37.84  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323   3 RAIPTFPCRDLDSASAFY-QSLGFHLGARY--------PTYAILQrgalelhLSLFEALEPKTNCSAAYLRLEDAQALHR 73
Cdd:cd07238   1 RIVANIATADPERAAAFYgDHLGLPLVMDHgwivtfasPGNAHAQ-------ISLAREGGSGTVVPDLSIEVDDVDAVHA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598323  74 QAAAlglgsQGIPRITALEDQPWGMREFALVDPDGNLLRV 113
Cdd:cd07238  74 RVVA-----AGLRIEYGPTTEAWGVRRFFVRDPFGRLINI 108
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 172-238 2.32e-03

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 37.25  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598323   172 LLWLAEAQQHPRGFVlahlwqiedGQARVGEIAELYVLPQARRQGLARELVGSAEEALRSRGAGLIR 238
Cdd:pfam13673  32 FFFVAFEGGQIVGVI---------ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSE 89
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 7-55 3.44e-03

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 36.49  E-value: 3.44e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15598323   7 TFPCRDLDSASAFYQS-LGFHLGARYPTYAILQRGALELHLSLFEALEPK 55
Cdd:cd07244   6 TLAVSDLERSLAFYVDlLGFKPHVRWDKGAYLTAGDLWLCLSLDPAAEPS 55
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 55-118 5.78e-03

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 403776  Cd Length: 118  Bit Score: 35.85  E-value: 5.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598323    55 KTNCSAAYLRLEDAQALHRQAAALGlgsqGIPRITALEDQPWGMREFALVDPDGNLLRVGQELD 118
Cdd:pfam12681  59 QSNNFELYFEVADVDAFLQKIKEIG----NIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
181-238 6.27e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 36.83  E-value: 6.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598323  181 HPRGFVlaHLWQIEDGQARVGEIAelyVLPQARRQGLARELVGSAEEALRSRGAGLIR 238
Cdd:PRK10975 112 QIQGFV--TLRELNDTDARIGLLA---VFPGAQGRGIGARLMQAALNWCQARGLTRLR 164
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-115 7.54e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 35.74  E-value: 7.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598323  11 RDLDSASAFYQ-SLGFHLGARYP-----TYAILQRGALE----LHLSLFEA-----LEPKTNCSAAYLRLEDAQALHRQA 75
Cdd:cd07263   7 DDQDKALDFYVeKLGFEVVEDVPmggmrWVTVAPPGSPGtsllLEPKAHPAqmpqsPEAAGGTPGILLATDDIDATYERL 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598323  76 AALGLgsqgipRITALEDQPWGMREFALVDPDGNLLRVGQ 115
Cdd:cd07263  87 TAAGV------TFVQEPTQMGGGRVANFRDPDGNLFALME 120
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 84-117 8.27e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319953  Cd Length: 122  Bit Score: 35.52  E-value: 8.27e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 15598323  84 GIPRITALEDQPWGMREFALVDPDGNLLRVGQEL 117
Cdd:cd09011  89 DIEFIHPILEHPWGQRVFRFYDPDGHIIEIGESM 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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