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Conserved domains on  [gi|669144918|ref|XP_008608021|]
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hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Saprolegnia diclina VS20]

Protein Classification

VOC family protein( domain architecture ID 10001243)

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
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-118 1.03e-20

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: 80.81  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSR-LGCSPIVVTE------TYARFEDGaGGSTFSLEKVDQEVPKMPGHHAMTMYFEVDDV 73
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDvLGLELVKRTDfgdggfGHAFLRLG-DGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 669144918  74 DATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLYYAGN 118
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-118 1.03e-20

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: 80.81  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSR-LGCSPIVVTE------TYARFEDGaGGSTFSLEKVDQEVPKMPGHHAMTMYFEVDDV 73
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDvLGLELVKRTDfgdggfGHAFLRLG-DGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 669144918  74 DATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLYYAGN 118
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-114 3.19e-15

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: 66.59  E-value: 3.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   7 TLPATDLPASIAFYSRLG---CSPIVVTETYARFEDGagGSTFSL---EKVDQEVPKMPGHHAMTMYFEVDDVDATVAAL 80
Cdd:cd07264    5 VLYVDDFAASLRFYRDVLglpPRFLHEEGEYAEFDTG--ETKLALfsrKEMARSGGPDRRGSAFELGFEVDDVEATVEEL 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 669144918  81 SAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLY 114
Cdd:cd07264   83 VERGAEFVREPANKPWGQTVAYVRDPDGNLIEIC 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-113 7.10e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 63.24  E-value: 7.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918    2 RFNQFTLPATDLPASIAFYSR-LGCSPIVVTE-------TYARFEDGAGGSTFSL-EKVDQEVPKMPGHHAMTMYFEVDD 72
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDvLGFKLVEETDageegglRSAFFLAGGRVLELLLnETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 669144918   73 VDATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCL 113
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-118 1.03e-20

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: 80.81  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSR-LGCSPIVVTE------TYARFEDGaGGSTFSLEKVDQEVPKMPGHHAMTMYFEVDDV 73
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDvLGLELVKRTDfgdggfGHAFLRLG-DGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 669144918  74 DATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLYYAGN 118
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-114 1.07e-17

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 73.13  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSR-LGCSPIVVTE---TYARFEDGaGGSTFSLEKVDQEvpkmPGHHAMTMYFEVDDVDAT 76
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEvFGWTFEDDAGpggDYAEFDTD-GGQVGGLMPGAEE----PGGPGWLLYFAVDDLDAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 669144918  77 VAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLY 114
Cdd:COG3324   78 VARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLW 115
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-114 3.19e-15

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: 66.59  E-value: 3.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   7 TLPATDLPASIAFYSRLG---CSPIVVTETYARFEDGagGSTFSL---EKVDQEVPKMPGHHAMTMYFEVDDVDATVAAL 80
Cdd:cd07264    5 VLYVDDFAASLRFYRDVLglpPRFLHEEGEYAEFDTG--ETKLALfsrKEMARSGGPDRRGSAFELGFEVDDVEATVEEL 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 669144918  81 SAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLY 114
Cdd:cd07264   83 VERGAEFVREPANKPWGQTVAYVRDPDGNLIEIC 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-113 7.10e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 63.24  E-value: 7.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918    2 RFNQFTLPATDLPASIAFYSR-LGCSPIVVTE-------TYARFEDGAGGSTFSL-EKVDQEVPKMPGHHAMTMYFEVDD 72
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDvLGFKLVEETDageegglRSAFFLAGGRVLELLLnETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 669144918   73 VDATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCL 113
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
8-116 3.24e-12

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 58.71  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   8 LPATDLPASIAFYSR-LGCSPIVVTET------YARFEdgAGGSTFSLEKVDQEVPKMPGHhAMTMYFEVDDVDATVAAL 80
Cdd:COG2764    6 LVVDDAEEALEFYEDvFGFEVVFRMTDpdgkimHAELR--IGGSVLMLSDAPPDSPAAEGN-GVSLSLYVDDVDALFARL 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 669144918  81 SAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLYYA 116
Cdd:COG2764   83 VAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-115 1.05e-11

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 58.05  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSR-LGCSPIVVTETYARFEDGAGGSTFSLEKVDQEVPKM--PGHHAMTmyFEVD---DVD 74
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDvLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAPPRPgaAGLDHVA--FRVPsraDLD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 669144918  75 ATVAALSAQGVVFDElPEDksWLWRES-RLRDPAGNRVCLYY 115
Cdd:COG2514   80 AALARLAAAGVPVEG-AVD--HGVGESlYFRDPDGNLIELYT 118
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-113 3.25e-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: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   6 FTLPATDLPASIAFY-SRLGCSPI--VVTETYARFEDGaGGSTFSLEKVDqEVPKMPGHHAMTMYFEVDDVDATVAALSA 82
Cdd:cd06587    2 VALRVPDLDASVAFYeEVLGFEVVsrNEGGGFAFLRLG-PGLRLALLEGP-EPERPGGGGLFHLAFEVDDVDEVDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 669144918  83 QGVVFD--ELPEDKSWLWRESRLRDPAGNRVCL 113
Cdd:cd06587   80 AGAEGElvAPPVDDPWGGRSFYFRDPDGNLIEF 112
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 6-114 3.28e-10

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: 53.42  E-value: 3.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   6 FTLPATDLPASIAFYSRL-GCSPIVVTE-----TYARFEDGAGGSTFsleKVDQEVPKMPGHhaMTMYFEVDDVDATVAA 79
Cdd:cd07247    4 FELPTTDLERAKAFYGAVfGWTFEDEGDgggdyALFTAGGGAVGGLM---RAPEEVAGAPPG--WLIYFAVDDLDAALAR 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 669144918  80 LSAQG--VVFDelPEDKSWLWRESRLRDPAGNRVCLY 114
Cdd:cd07247   79 VEAAGgkVVVP--PTDIPGGGRFAVFADPEGNRFGLW 113
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 8-112 1.60e-09

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: 51.84  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   8 LPATDLPASIAFYSR-LGcspivVTETYARFEDG-----AGGSTFSLEKVDQEVPKMPGHHAmtmYFEVDDVDATVAALS 81
Cdd:cd08349    4 LPVRDIDKTLAFYVDvLG-----FEVDYERPPPGyailsRGGVELHLFEHPGLDPAGSGVAA---YIRVEDIDALHAELK 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 669144918  82 AQGVVFDELP-----EDKSWLWRESRLRDPAGNRVC 112
Cdd:cd08349   76 AAGLPLFGIPritpiEDKPWGMREFAVVDPDGNLLR 111
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 5-113 1.23e-06

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 44.29  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918    5 QFTLPATDLPASIAFYSRLGCSPIVVTETYARFEDGA-----GGSTFSLEKVDQEVP-KMPGHhamtMYFEVDDVDATVA 78
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPDPDGGgpiggGGPRLLFQRVPEPKPgKNRVH----LDLAVDDLEAAVA 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 669144918   79 ALSAQGVVfdELPEDKSWLWRESRLRDPAGNRVCL 113
Cdd:pfam18029  77 RLVALGAT--VLDDGDDPDGGRWVLADPEGNEFCL 109
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 42-110 1.85e-06

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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 43.82  E-value: 1.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669144918  42 GGSTFSL--EKVDQEVPKMPGHHAM--TMYFEVDDVDATVA-ALSAQGVVFDElPEDKSWLWRESRLRDPAGNR 110
Cdd:cd07246   46 GGTVVMVadENPERGALSPTKLGGTpvIFHLYVEDVDATFArAVAAGAVVVEP-VEDQFWGDRVGKVKDPFGHV 118
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 9-108 5.28e-06

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: 42.29  E-value: 5.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   9 PATDLPASIAFYSRLGCSPIVVTETYARFEDGAggSTFSLEKVDQEvpkmpgHHA--MTMYFEVDDVDATVAALSAQGVV 86
Cdd:cd08356    8 PAKDFELSKAFYQALGFELASEEGGVAYFRLGD--CSFLLQDFYEK------EHAenFMMHLLVEDVDAWHQHVKTLGLA 79

                         90       100
                 ....*....|....*....|....*..
gi 669144918  87 FD-----ELPEDKSWLWRESRLRDPAG 108
Cdd:cd08356   80 ERygvkvTDPTDQPWGMRDFVLTDPSG 106
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-96 1.09e-05

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 41.74  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSRLGCS--PIVVTETYARFeDGAGGSTFSL-------EKVDQEVPKMPGHHAMTMYFEVD 71
Cdd:COG3607    2 PRIIFVNLPVADLERSRAFYEALGFTfnPQFSDEGAACF-VLGEGIVLMLlprekfaTFTGKPIADATGFTEVLLALNVE 80

                         90       100
                 ....*....|....*....|....*...
gi 669144918  72 ---DVDATVAALSAQGVVFDELPEDKSW 96
Cdd:COG3607   81 sreEVDALVAKALAAGGTVLKPPQDVGG 108
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 68-108 4.38e-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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 40.07  E-value: 4.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 669144918  68 FEVDDVDATVAALSAQGVVFDELPEDKSWLWRESRLRDPAG 108
Cdd:cd08359   72 FEVDDADAEYERLTQAGLEFLEPPRDEPWGQRRFIVRDPNG 112
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-109 5.52e-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: 319953  Cd Length: 122  Bit Score: 39.76  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   1 MRFNQFTLPATDLPASIAFYSRLGCSPI-------VVTETYARFEDGAGGSTFsLEKVDQEVPKmpGHHAMTMYFEVDDV 73
Cdd:cd09011    1 MKFVNPLLVVKDIEKSKKFYEDVLGQKIlldfgenVVFEGGFALQEKKSWLET-IIISDLSIKQ--QSNNFELYFEVDDF 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 669144918  74 DATVAALSA-QGVVFDELPEDKSWLWRESRLRDPAGN 109
Cdd:cd09011   78 DAFFEKLNPhKDIEFIHPILEHPWGQRVFRFYDPDGH 114
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-115 1.38e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 38.75  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   3 FNQFTLPATDLPASIAFY----SRLGCSPIVVTETYARFEDGAGGStFSLEKVDQEVPKMPGHHAMTMyFEVDD---VDA 75
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYdaalAPLGYKRGFEDGGRVGYGLEGGPD-FWVTEPFDGEPATAGNGTHVA-FAAPSraaVDA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 669144918  76 -TVAALSAQGVvfdelPEDKSWLWRESR-------LRDPAGNRVCLYY 115
Cdd:cd07262   79 fHAAALAAGGT-----DNGAPGLRPHYHpgyyaayVRDPDGNKIEAVC 121
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-115 2.96e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 37.83  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   5 QFTLPATDLPASIAFYSRL-GCSPIVVTETYARFEDGAGGSTFSLEKVDQEVPKMPGHhamtMYFEVDDVDATVA----A 79
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLfGAEPAKRKADYAKFMLEDPPLNLALLVNDRKEPYGLNH----LGIQVDSKEEVAAlkarA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 669144918  80 LSAQGVVFDEL-------PEDKSWlwresrLRDPAGNRVCLYY 115
Cdd:cd07254   80 EAAGLPVRKEPrttccyaVQDKFW------LTDPDGNAWEFYA 116
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 3-85 5.28e-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: 37.26  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   3 FNQFTLPATDLPASIAFYSR-LGCSPIVVTETYARFEdgAGGSTFSLEkVDQEVPKMP--GHHAMTmyFEVDDVDATVAA 79
Cdd:cd07244    2 INHITLAVSDLERSLAFYVDlLGFKPHVRWDKGAYLT--AGDLWLCLS-LDPAAEPSPdyTHIAFT--VSEEDFEELSER 76


                 ....*.
gi 669144918  80 LSAQGV 85
Cdd:cd07244   77 LRAAGV 82
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 3-114 5.72e-04

Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes.


Pssm-ID: 319901  Cd Length: 123  Bit Score: 37.09  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918   3 FNQFTLPATDLPASIAFYSRLG------CSPIVVTEtyARFEDGAGGSTFSLEKV---DQEVPKMPGHHAMTMYFEVD-- 71
Cdd:cd07235    1 ISLIAIVVEDMAKSLEFYRKLGfevpeeADSAPHTE--AALPGGIRLALDTEETIrsyDPGWQAPTGGGRFAIAFLCPtp 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 669144918  72 -DVDATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRVCLY 114
Cdd:cd07235   79 aEVDAKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNVVDLF 122
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 3-109 7.18e-04

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 37.01  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918    3 FNQFTLPATDLPASIAFYSRLGCSPIVVTE-TYARFEDGAGGSTFSLEKVDQEVPKMPGHHAMTMYFEVDDVDATVAALS 81
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFgENVSFEGGFAIQSDFKELIGIDLSIAEQSNNFELYFEVADVDAFLQKIK 80

                          90       100
                  ....*....|....*....|....*....
gi 669144918   82 AQGVV-FDELPEDKSWLWRESRLRDPAGN 109
Cdd:pfam12681  81 EIGNIeYLHELKEQPWGQRVFRFYDPDGH 109
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 12-87 9.87e-04

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: 36.22  E-value: 9.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669144918  12 DLPASIAFYSRL-GCSPIVVTETYARFEDGaGGSTFSLEKVDQEVPK-MPGHHAMTMYFEV---DDVDATVAALSAQGVV 86
Cdd:cd07261    8 NPERSTEFYRFLlGKEPVESSPTFASFVLS-GGAKLGLWSSEEVEPKvAVTGGGAELSFMVpsgEQVDEVYAEWKAMGIP 86


                 .
gi 669144918  87 F 87
Cdd:cd07261   87 I 87
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 66-111 1.12e-03

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: 36.32  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 669144918  66 MYFEV--DDVDATVAALSAQGVVFDELPEDKSWLWRESRLRDPAGNRV 111
Cdd:cd16355   70 AWMSVwvDDVDALHRECRARGADIRQPPTDMPWGMREMHVRHPDGHRF 117
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 61-87 5.20e-03

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 34.47  E-value: 5.20e-03
                         10        20
                 ....*....|....*....|....*..
gi 669144918  61 HHamtMYFEVDDVDATVAALSAQGVVF 87
Cdd:cd07249   73 HH---IAFEVDDIDAAVEELKAQGVRL 96
 
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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