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Conserved domains on  [gi|495000355|ref|WP_007726371|]
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MULTISPECIES: VOC family protein [Bacillales]

Protein Classification

VOC family protein( domain architecture ID 11457526)

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
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-130 8.26e-19

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


:

Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 76.54  E-value: 8.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   4 LKAVHHIALNCSDVVKVARFFKDILEVPIPEEnmtEGAPVYFQI-GTYTRIGLHPHGGEAGKGGVGQVDHLAFSVQSRAE 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVER---EGGRVYLRAdGGEHLLVLEEAPGAPPRPGAAGLDHVAFRVPSRAD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495000355  83 LDYLVDKLEAENICYRGPITQPTSYNLYFETPDGHHLEVRLDKDEFDE 130
Cdd:COG2514   78 LDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEH 125
 
Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-130 8.26e-19

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 76.54  E-value: 8.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   4 LKAVHHIALNCSDVVKVARFFKDILEVPIPEEnmtEGAPVYFQI-GTYTRIGLHPHGGEAGKGGVGQVDHLAFSVQSRAE 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVER---EGGRVYLRAdGGEHLLVLEEAPGAPPRPGAAGLDHVAFRVPSRAD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495000355  83 LDYLVDKLEAENICYRGPITQPTSYNLYFETPDGHHLEVRLDKDEFDE 130
Cdd:COG2514   78 LDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEH 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-121 2.53e-10

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: 53.68  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   9 HIALNCSDVVKVARFFKDILEVPIPEENMTEGApVYFQIGTYTRIGLHPHGGEAGKGGVGqVDHLAFSVQSRAELDYLVD 88
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF-AFLRLGPGLRLALLEGPEPERPGGGG-LFHLAFEVDDVDEVDERLR 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495000355  89 KLEAENICYRGPITQP-TSYNLYFETPDGHHLEV 121
Cdd:cd06587   79 EAGAEGELVAPPVDDPwGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-121 3.58e-05

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.51  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355    7 VHHIALNCSDVVKVARFFKDIL------EVPIPEENMTEGApvYFQIGTyTRIGLHPHGGEAGKGGVGQVDHLAFSVQSR 80
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLgfklveETDAGEEGGLRSA--FFLAGG-RVLELLLNETPPPAAAGFGGHHIAFIAFSV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 495000355   81 AELDYLVDKLEAENI-CYRGPITQP-TSYNLYFETPDGHHLEV 121
Cdd:pfam00903  79 DDVDAAYDRLKAAGVeIVREPGRHGwGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-130 8.26e-19

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 76.54  E-value: 8.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   4 LKAVHHIALNCSDVVKVARFFKDILEVPIPEEnmtEGAPVYFQI-GTYTRIGLHPHGGEAGKGGVGQVDHLAFSVQSRAE 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVER---EGGRVYLRAdGGEHLLVLEEAPGAPPRPGAAGLDHVAFRVPSRAD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495000355  83 LDYLVDKLEAENICYRGPITQPTSYNLYFETPDGHHLEVRLDKDEFDE 130
Cdd:COG2514   78 LDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEH 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-121 1.47e-15

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: 67.71  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   7 VHHIALNCSDVVKVARFFKDILE-VPIPEENMTEGAP--VYFQIGTYTRIGLHPHGGEAGKGGVGQVDHLAFSVqsrAEL 83
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGlELVKRTDFGDGGFghAFLRLGDGTELELFEAPGAAPAPGGGGLHHLAFRV---DDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495000355  84 DYLVDKLEAENI-CYRGPITQPT-SYNLYFETPDGHHLEV 121
Cdd:COG0346   80 DAAYARLRAAGVeIEGEPRDRAYgYRSAYFRDPDGNLIEL 119
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-121 2.53e-10

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: 53.68  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   9 HIALNCSDVVKVARFFKDILEVPIPEENMTEGApVYFQIGTYTRIGLHPHGGEAGKGGVGqVDHLAFSVQSRAELDYLVD 88
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF-AFLRLGPGLRLALLEGPEPERPGGGG-LFHLAFEVDDVDEVDERLR 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495000355  89 KLEAENICYRGPITQP-TSYNLYFETPDGHHLEV 121
Cdd:cd06587   79 EAGAEGELVAPPVDDPwGGRSFYFRDPDGNLIEF 112
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 15-121 7.12e-09

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 50.21  E-value: 7.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355  15 SDVVKVARFFKDI-LEvpiPEENMTEGAPVYFQIGTYTRIGLHPHGGEAGKGGVGQVDH-------LAFSVQSRAELDYL 86
Cdd:COG3607   12 ADLERSRAFYEALgFT---FNPQFSDEGAACFVLGEGIVLMLLPREKFATFTGKPIADAtgftevlLALNVESREEVDAL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495000355  87 VDKLEAEnicyRGPITQPTS-----YNLYFETPDGHHLEV 121
Cdd:COG3607   89 VAKALAA----GGTVLKPPQdvggmYSGYFADPDGHLWEV 124
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-121 3.84e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 45.39  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   7 VHHIALNCSDVVKVARFFKDIL---EVPIPEENMTEGApvYFQIGtyTRIGLH-----PHGGEAGKGGVGQVDHLAFSVQ 78
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLgleEVPRPPFLKFGGA--WLYLG--GGQQIHlvveqNPSELPRPEHPGRDRHPSFSVP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495000355  79 SraeLDYLVDKLEAENICYR------GPITQptsynLYFETPDGHHLEV 121
Cdd:cd07245   77 D---LDALKQRLKEAGIPYTestspgGGVTQ-----LFFRDPDGNRLEF 117
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 6-121 1.16e-05

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 41.70  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   6 AVHHIALNCSDVVKVARFFKDILEVPIPEENMTEGAPVYFQIGTY-----------------TRIGLHphggeagkggvg 68
Cdd:cd07242    1 GVSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGPSWKLSGGSllvvqqtdefatpefdrARVGLN------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495000355  69 qvdHLAFSVQSRAELDYLVDKLEAENicyrGPITQ---------PTSYNLYFETPDGHHLEV 121
Cdd:cd07242   69 ---HLAFHAESREAVDELTEKLAKIG----GVRTYgdrhpfaggPPHYAAFCEDPDGIKLEL 123
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-121 3.58e-05

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.51  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355    7 VHHIALNCSDVVKVARFFKDIL------EVPIPEENMTEGApvYFQIGTyTRIGLHPHGGEAGKGGVGQVDHLAFSVQSR 80
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLgfklveETDAGEEGGLRSA--FFLAGG-RVLELLLNETPPPAAAGFGGHHIAFIAFSV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 495000355   81 AELDYLVDKLEAENI-CYRGPITQP-TSYNLYFETPDGHHLEV 121
Cdd:pfam00903  79 DDVDAAYDRLKAAGVeIVREPGRHGwGGRYSYFRDPDGNLIEL 121
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 9-121 5.16e-05

ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins; ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP 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.


Pssm-ID: 319939  Cd Length: 118  Bit Score: 39.80  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   9 HIALNCSDVVKVARFFKDILEVPIPEE-------NMTEGAPVYFQIgtyTRIGLHPHggeagkggvgqvdHLAFSVqSRA 81
Cdd:cd08351    5 HTIVPARDKEASARFLAEILGLPAPPPwgpfapvRLNNGLTLDFAD---PRGEIAPQ-------------HYAFLV-SDD 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495000355  82 ELDYLVDKLEAENICYR-GPI-TQPTSYN-------LYFETPDGHHLEV 121
Cdd:cd08351   68 EFDAILARIRARGLEYWaDPQhREPGEINhndggrgVYFRDPDGHLLEI 116
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 7-121 4.09e-04

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 37.61  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   7 VHHIALNCSDVVKVARFFKDI--LEVPIPEENMtegapVYFQIGtytriGLHPHGGEAGKGGVGQVDHLAFSVQSRAELD 84
Cdd:cd08362    4 LRYVALGVPDLAAEREFYTEVwgLEEVAEDDDV-----VYLRAE-----GSEHHVLRLRQSDENRLDLIAFAAATRADVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495000355  85 YLVDKLEAEN---ICYRGPITQPTS-YNLYFETPDGHHLEV 121
Cdd:cd08362   74 ALAARLAAAGvriLSEPGPLDDPGGgYGFRFFDPDGRTIEV 114
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 9-121 5.98e-04

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: 36.88  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   9 HIALNCSDVVKVARFFKDILEVpIPEENMTEGApvYFQIGT-YTRIGLHPHGGEAGKGgvgqvDHLAFSVqSRAELDYLV 87
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGF-KPHVRWDKGA--YLTAGDlWLCLSLDPAAEPSPDY-----THIAFTV-SEEDFEELS 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495000355  88 DKLEAENI-CYRgpitQPTS--YNLYFETPDGHHLEV 121
Cdd:cd07244   75 ERLRAAGVkIWQ----ENSSegDSLYFLDPDGHKLEL 107
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-121 7.71e-04

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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 36.89  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355  10 IALNCSDVVKVARFFKDIlevPIPEENMTEGAPVYFQIGTYTrIGLHPhGGEAGKGGVGQVDH-------LAFSVQSRAE 82
Cdd:cd07251    2 ITLGVRDLERSARFYEAL---GWKPNLDPNDGVVFFQLGGTV-LALYP-RDALAEDAGVSVTGagfsgvtLAHNVRSREE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495000355  83 LDYLVDKLEAENicyrGPITQPTS------YNLYFETPDGHHLEV 121
Cdd:cd07251   77 VDQLLAKAVAAG----GKILKPPQevfwggYSGYFADPDGHIWEV 117
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 70-126 8.27e-03

N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the N-terminal domain.


Pssm-ID: 319926  Cd Length: 122  Bit Score: 33.86  E-value: 8.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495000355  70 VDHLAFSVQSRAELDYLVDKLEAenicYRGPITQ-------PTSYNLYFETPDGHHLEVRLDKD 126
Cdd:cd07265   62 LDFMGFKVLDDADLEQLEARLQA----YGVTVTRipagelpGVGRRVRFQLPSGHTMELYAEKE 121
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-126 9.69e-03

N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the N-terminal repeat.


Pssm-ID: 319955  Cd Length: 121  Bit Score: 33.86  E-value: 9.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495000355   2 FHLKAVHHIALNCSDVVKVARFFKDILEVpipEENMTEGAPVYFQI-GTYtriglHPHGGEAGKGGVGQVDHLAFSVQSR 80
Cdd:cd09013    2 FDLAQLAHVELLTPKPEESLWFFTDVLGL---EETHREGQSVYLRAwGDW-----EHHTLKLTESPEAGLGHIAWRASSP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495000355  81 AELDYLVDKLEAENICYR---GPITQPTSYNlyFETPDGHHLEVRLDKD 126
Cdd:cd09013   74 EALERRVAALEASGVGIGwidGDLGQGPAYR--FQSPDGHPMEIYWEVE 120
 
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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