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Conserved domains on  [gi|1159783463|ref|WP_079327913|]
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VOC family protein [Stutzerimonas stutzeri]

Protein Classification

VOC family protein( domain architecture ID 10007568)

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
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-141 1.23e-94

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


:

Pssm-ID: 442786  Cd Length: 139  Bit Score: 268.97  E-value: 1.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   1 MTLSPFHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEAPKMPhqEAAHSNPVDGHDVPVPHFGVVL 80
Cdd:COG3565     1 MMLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFA--FTAATNPVDGHDVPVPHFGVVL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159783463  81 GWEQWEALAERLKARGTRFVIEPYVRFQGQVGEQATMFLLDPCGNALEFKAFKDIGQLFAK 141
Cdd:COG3565    79 DWDDWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK 139
 
Name Accession Description Interval E-value
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-141 1.23e-94

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


Pssm-ID: 442786  Cd Length: 139  Bit Score: 268.97  E-value: 1.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   1 MTLSPFHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEAPKMPhqEAAHSNPVDGHDVPVPHFGVVL 80
Cdd:COG3565     1 MMLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFA--FTAATNPVDGHDVPVPHFGVVL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159783463  81 GWEQWEALAERLKARGTRFVIEPYVRFQGQVGEQATMFLLDPCGNALEFKAFKDIGQLFAK 141
Cdd:COG3565    79 DWDDWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK 139
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 6-132 8.31e-68

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 200.69  E-value: 8.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   6 FHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEAPKMPhqeAAHSNPVDGHDVPVPHFGVVLGWEQW 85
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYA---STSTNAVDGHSVPVPHFGLALTVDDF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1159783463  86 EALAERLKARGTRFVIEPYVRFQGQVGEQATMFLLDPCGNALEFKAF 132
Cdd:cd08357    78 DALAERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-129 4.25e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 53.61  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEApkmpHQEAAHSNPVDGHDVPVPHFGV---VLGWE 83
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR----VLELLLNETPPPAAAGFGGHHIafiAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1159783463  84 QWEALAERLKARGTRFVIEPyvrfQGQVGEQATMFLLDPCGNALEF 129
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREP----GRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-141 1.23e-94

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


Pssm-ID: 442786  Cd Length: 139  Bit Score: 268.97  E-value: 1.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   1 MTLSPFHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEAPKMPhqEAAHSNPVDGHDVPVPHFGVVL 80
Cdd:COG3565     1 MMLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFA--FTAATNPVDGHDVPVPHFGVVL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159783463  81 GWEQWEALAERLKARGTRFVIEPYVRFQGQVGEQATMFLLDPCGNALEFKAFKDIGQLFAK 141
Cdd:COG3565    79 DWDDWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK 139
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 6-132 8.31e-68

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 200.69  E-value: 8.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   6 FHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEAPKMPhqeAAHSNPVDGHDVPVPHFGVVLGWEQW 85
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYA---STSTNAVDGHSVPVPHFGLALTVDDF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1159783463  86 EALAERLKARGTRFVIEPYVRFQGQVGEQATMFLLDPCGNALEFKAF 132
Cdd:cd08357    78 DALAERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-129 1.80e-11

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: 57.31  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTEGR---SSDHWVDFDFF----GHQLVIHEAPKMPHQEAAHSnpvdghdvpVPHFGvv 79
Cdd:COG0346     5 HVTLRVSDLEASLAFYTDVLGLELVKrtdFGDGGFGHAFLrlgdGTELELFEAPGAAPAPGGGG---------LHHLA-- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1159783463  80 LGWEQWEALAERLKARGTRFVIEPYVRFQGQVgeqaTMFLLDPCGNALEF 129
Cdd:COG0346    74 FRVDDLDAAYARLRAAGVEIEGEPRDRAYGYR----SAYFRDPDGNLIEL 119
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-129 4.89e-11

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 56.18  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   1 MTLSPFHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFF----GHQLVIHEAPKMPhqeaahsnpvdGHDVPVPHF 76
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFdtdgGQVGGLMPGAEEP-----------GGPGWLLYF 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1159783463  77 GVvlgwEQWEALAERLKARGTRFVIEPYvrfqgQVGEQATMFLL-DPCGNALEF 129
Cdd:COG3324    70 AV----DDLDAAVARVEAAGGTVLRPPT-----DIPPWGRFAVFrDPEGNRFGL 114
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-129 4.25e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 53.61  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFGHQLVIHEApkmpHQEAAHSNPVDGHDVPVPHFGV---VLGWE 83
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR----VLELLLNETPPPAAAGFGGHHIafiAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1159783463  84 QWEALAERLKARGTRFVIEPyvrfQGQVGEQATMFLLDPCGNALEF 129
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREP----GRHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
7-134 2.11e-09

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 52.27  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFFG--HQLVIHEAPKMPHQEAAHSnpvdghdvpVPHFGV-VLGWE 83
Cdd:COG2514     6 HVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGgeHLLVLEEAPGAPPRPGAAG---------LDHVAFrVPSRA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1159783463  84 QWEALAERLKARGtrfviepyVRFQGQV--GEQATMFLLDPCGNALEFKAFKD 134
Cdd:COG2514    77 DLDAALARLAAAG--------VPVEGAVdhGVGESLYFRDPDGNLIELYTDRP 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-129 5.05e-09

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: 50.60  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTE--GRSSDHWVDFDFF-GHQLVIHEAPkmphqeaahsNPVDGHDVPVPHFGVVLgwE 83
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGpGLRLALLEGP----------EPERPGGGGLFHLAFEV--D 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1159783463  84 QWEALAERLKARGTRFVIEPYVRfqGQVGEQATMFLLDPCGNALEF 129
Cdd:cd06587    69 DVDEVDERLREAGAEGELVAPPV--DDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-129 1.31e-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: 46.93  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTEGRSSDHwvdFDFFGHQLVIHEAPKMpH--QEAAHSNPVDGHDVP-VPHFGVVLgwE 83
Cdd:cd07245     3 HVALACPDLERARRFYTDVLGLEEVPRPPF---LKFGGAWLYLGGGQQI-HlvVEQNPSELPRPEHPGrDRHPSFSV--P 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1159783463  84 QWEALAERLKARGTrfviePYVRFQGQVGEQATMFLLDPCGNALEF 129
Cdd:cd07245    77 DLDALKQRLKEAGI-----PYTESTSPGGGVTQLFFRDPDGNRLEF 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-129 2.01e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 46.56  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCTEGRSSD--HWVDFDFFGHQLVIheapkMPHQEAAHSnpvDGHDVPVPHFGVVLGWEQ 84
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEegEYAEFDTGETKLAL-----FSRKEMARS---GGPDRRGSAFELGFEVDD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1159783463  85 WEALAERLKARGTRFVIEPYVRFQGqvgeQATMFLLDPCGNALEF 129
Cdd:cd07264    75 VEATVEELVERGAEFVREPANKPWG----QTVAYVRDPDGNLIEI 115
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 7-130 8.27e-05

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. 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: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 39.52  E-value: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   7 HLAIPVYDLAAARAFYGEAFGCT-----EGRSSDHwvdfdfFGHQLV-IHEApKMPHQEAAHsNPVDGHDvpvpHFGVVL 80
Cdd:cd07253     6 HLVLTVKDIERTIDFYTKVLGMTvvtfkEGRKALR------FGNQKInLHQK-GKEFEPKAS-APTPGSA----DLCFIT 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1159783463  81 GwEQWEALAERLKARGTRfVIEPYVRFQGQVGEQATMFLLDPCGNALEFK 130
Cdd:cd07253    74 E-TPIDEVLEHLEACGVT-IEEGPVKRTGALGPILSIYFRDPDGNLIELS 121
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 10-127 2.50e-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: 38.01  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463  10 IPVYDLAAARAFYGEAFGCTEGRSSDHWVDFDFF--GHQLV--IHEAPKMPHQEAAHsnpvdghdvPVPHFGVvlgwEQW 85
Cdd:cd07247     6 LPTTDLERAKAFYGAVFGWTFEDEGDGGGDYALFtaGGGAVggLMRAPEEVAGAPPG---------WLIYFAV----DDL 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1159783463  86 EALAERLKARGTRFVIEPYvrfqgQVGEQATMFLL-DPCGNAL 127
Cdd:cd07247    73 DAALARVEAAGGKVVVPPT-----DIPGGGRFAVFaDPEGNRF 110
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-129 2.83e-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: 38.21  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159783463   6 FHLAIPVYDLAAARAFYGEAFGCTEGRSSDHWVDF--DFFGHQLVIHEAPKMPHQEaahsnpvdghdvpVPHFGV-VLGW 82
Cdd:cd07254     3 FHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFmlEDPPLNLALLVNDRKEPYG-------------LNHLGIqVDSK 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1159783463  83 EQWEALAERLKARGTRFVIEPYVRFQGQVGEQatMFLLDPCGNALEF 129
Cdd:cd07254    70 EEVAALKARAEAAGLPVRKEPRTTCCYAVQDK--FWLTDPDGNAWEF 114
 
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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