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Conserved domains on  [gi|684994532|gb|KGA32234|]
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drug:proton antiporter [Pectobacterium brasiliense]

Protein Classification

VOC family protein( domain architecture ID 50733)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-118 5.43e-48

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.


The actual alignment was detected with superfamily member cd07261:

Pssm-ID: 472697  Cd Length: 114  Bit Score: 149.47  E-value: 5.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   6 FIILYVEDAVTSERFYRELFDFQPVEKSENFAMFAFDSGLLLGLWSKHEVKPLTQLAGGGSELAIRVESEVALNAIYENW 85
Cdd:cd07261    1 LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSGEQVDEVYAEW 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 684994532  86 KARDITIAQDITQMDFGLTFVALDPDHHRLRVY 118
Cdd:cd07261   81 KAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVC 113
 
Name Accession Description Interval E-value
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 6-118 5.43e-48

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 149.47  E-value: 5.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   6 FIILYVEDAVTSERFYRELFDFQPVEKSENFAMFAFDSGLLLGLWSKHEVKPLTQLAGGGSELAIRVESEVALNAIYENW 85
Cdd:cd07261    1 LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSGEQVDEVYAEW 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 684994532  86 KARDITIAQDITQMDFGLTFVALDPDHHRLRVY 118
Cdd:cd07261   81 KAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVC 113
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-119 1.20e-18

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 75.25  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   1 MNAPNFIILYVEDAVTSERFYREL-FDFQPVEKSENFAMFAFDSGLLLGLWSKHEVKPLTQL----AGGGSE--LAIRVE 73
Cdd:COG3607    1 MPRIIFVNLPVADLERSRAFYEALgFTFNPQFSDEGAACFVLGEGIVLMLLPREKFATFTGKpiadATGFTEvlLALNVE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 684994532  74 SEVALNAIYENWKARDITIAQDITQMDFGLTFVALDPDHHRLRVYY 119
Cdd:COG3607   81 SREEVDALVAKALAAGGTVLKPPQDVGGMYSGYFADPDGHLWEVAW 126
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-117 1.72e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 38.20  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532    5 NFIILYVEDAVTSERFYRELFDFQPVEKSEN------FAMFAFDSGLLLGLWSKHEVKPLTQLAGGGSeLAIRVESEVAL 78
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGFKLVEETDAgeegglRSAFFLAGGRVLELLLNETPPPAAAGFGGHH-IAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 684994532   79 NAIYENWKARDITIAQDITQMDFG-LTFVALDPDHHRLRV 117
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWGgRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 6-118 5.43e-48

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 149.47  E-value: 5.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   6 FIILYVEDAVTSERFYRELFDFQPVEKSENFAMFAFDSGLLLGLWSKHEVKPLTQLAGGGSELAIRVESEVALNAIYENW 85
Cdd:cd07261    1 LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSGEQVDEVYAEW 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 684994532  86 KARDITIAQDITQMDFGLTFVALDPDHHRLRVY 118
Cdd:cd07261   81 KAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVC 113
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-119 1.20e-18

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 75.25  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   1 MNAPNFIILYVEDAVTSERFYREL-FDFQPVEKSENFAMFAFDSGLLLGLWSKHEVKPLTQL----AGGGSE--LAIRVE 73
Cdd:COG3607    1 MPRIIFVNLPVADLERSRAFYEALgFTFNPQFSDEGAACFVLGEGIVLMLLPREKFATFTGKpiadATGFTEvlLALNVE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 684994532  74 SEVALNAIYENWKARDITIAQDITQMDFGLTFVALDPDHHRLRVYY 119
Cdd:COG3607   81 SREEVDALVAKALAAGGTVLKPPQDVGGMYSGYFADPDGHLWEVAW 126
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-119 2.98e-14

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: 63.86  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   7 IILYVEDAVTSERFYRELFDFQPVEKSEN------FAMFAFDSGLLLGLWSKHEVKPLTQlAGGGSELAIRVEsevALNA 80
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTDFgdggfgHAFLRLGDGTELELFEAPGAAPAPG-GGGLHHLAFRVD---DLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 684994532  81 IYENWKARDITIAQDITQMDFGLTFVAL-DPDHHRLRVYY 119
Cdd:COG0346   82 AYARLRAAGVEIEGEPRDRAYGYRSAYFrDPDGNLIELVE 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-118 1.73e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 59.26  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   1 MNAPNFIILYVEDAVTSERFYRELFDFQPVEKSE---NFAMFAFDSGLLLGLWSKHEVKpltqlAGGGSELAIRVESeva 77
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGGQVGGLMPGAEEP-----GGPGWLLYFAVDD--- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 684994532  78 LNAIYENWKARDITIAQDITQM-DFGLTFVALDPDHHRLRVY 118
Cdd:COG3324   74 LDAAVARVEAAGGTVLRPPTDIpPWGRFAVFRDPEGNRFGLW 115
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-117 1.18e-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: 57.15  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   7 IILYVEDAVTSERFYRELFDFQPVEKSE--NFAMFAFDSGLLLGLWSKHEVKPLTqlAGGGSELAIRVESEVALNAIYEN 84
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSRNEggGFAFLRLGPGLRLALLEGPEPERPG--GGGLFHLAFEVDDVDEVDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 684994532  85 WKARDITIAQDITQMDFGLTFVALDPDHHRLRV 117
Cdd:cd06587   80 AGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-113 4.37e-11

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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 55.42  E-value: 4.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   6 FIILYVEDAVTSERFYRELFDFQPVEKSEN--FAMFaFDSGLLLGLWSKHEVKPLT--QLAGGGSELAIRVESevaLNAI 81
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEF-DTGETKLALFSRKEMARSGgpDRRGSAFELGFEVDD---VEAT 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 684994532  82 YENWKARDITIAQDITQMDFGLT-FVALDPDHH 113
Cdd:cd07264   79 VEELVERGAEFVREPANKPWGQTvAYVRDPDGN 111
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
7-119 4.56e-09

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 50.73  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   7 IILYVEDAVTSERFYRELFDFQPVEKSENFAMFAFDSGL-LLGLWsKHEVKPLTQLAGGGSELAIRVESEVALNAIYENW 85
Cdd:COG2514    7 VTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEhLLVLE-EAPGAPPRPGAAGLDHVAFRVPSRADLDAALARL 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 684994532  86 KARDITIaQDITQMDFGLTFVALDPDHHRLRVYY 119
Cdd:COG2514   86 AAAGVPV-EGAVDHGVGESLYFRDPDGNLIELYT 118
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-120 6.38e-06

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 42.15  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   7 IILYVEDAVTSERFYRELFDFQPVEKSEN------FAMFAFDsGLLLGLWSKHEVKPLTqlAGGGSELAIRVEsEVAlnA 80
Cdd:COG2764    4 PYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIG-GSVLMLSDAPPDSPAA--EGNGVSLSLYVD-DVD--A 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 684994532  81 IYENWKARDITIAQDITQMDFGLTFVAL-DPDHHRLRVYYA 120
Cdd:COG2764   78 LFARLVAAGATVVMPLQDTFWGDRFGMVrDPFGVLWMINTP 118
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-111 1.40e-05

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: 41.13  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   7 IILYVEDAVTSERFYRELFDFQPVEKSENFAMF--------AFDSGLLLGLWSKHEVKPLTQLAGGGSElAIRVESEvAL 78
Cdd:cd07263    2 VMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRwvtvappgSPGTSLLLEPKAHPAQMPQSPEAAGGTP-GILLATD-DI 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 684994532  79 NAIYENWKARDITIAQDITQMDFGLTFVALDPD 111
Cdd:cd07263   80 DATYERLTAAGVTFVQEPTQMGGGRVANFRDPD 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-117 1.72e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 38.20  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532    5 NFIILYVEDAVTSERFYRELFDFQPVEKSEN------FAMFAFDSGLLLGLWSKHEVKPLTQLAGGGSeLAIRVESEVAL 78
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGFKLVEETDAgeegglRSAFFLAGGRVLELLLNETPPPAAAGFGGHH-IAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 684994532   79 NAIYENWKARDITIAQDITQMDFG-LTFVALDPDHHRLRV 117
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWGgRYSYFRDPDGNLIEL 121
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-119 1.24e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 35.90  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 684994532   9 LYVEDAVTSERFYRELFDFQPVEKSENFAMFAF-DSGLLLGLWSKHEVKPltqlaGGGSELAIRVESEVALNAIYENWKA 87
Cdd:cd07254    7 LNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLeDPPLNLALLVNDRKEP-----YGLNHLGIQVDSKEEVAALKARAEA 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 684994532  88 RDITIAQDI-------TQMDFGLTfvalDPDHHRLRVYY 119
Cdd:cd07254   82 AGLPVRKEPrttccyaVQDKFWLT----DPDGNAWEFYA 116
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-75 1.95e-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: 319942  Cd Length: 122  Bit Score: 35.42  E-value: 1.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 684994532   8 ILYVEDAVTSERFYRELFDFQPVEKSENFAMFAFDSGLLLGLWSKHEVKPLTQLAG------GGSELAIRVESE 75
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVFDPGATSKDVRTGEVpghgasGHGHFAFAVPTE 78
 
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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