##gff-version 3 P0A006 UniProtKB Chain 1 131 . . . ID=PRO_0000162523;Note=Arsenate reductase P0A006 UniProtKB Active site 10 10 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_01624,ECO:0000305|PubMed:11573087,ECO:0000305|PubMed:12072565;Dbxref=PMID:11573087,PMID:12072565 P0A006 UniProtKB Active site 82 82 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_01624,ECO:0000305|PubMed:11573087,ECO:0000305|PubMed:12072565;Dbxref=PMID:11573087,PMID:12072565 P0A006 UniProtKB Active site 89 89 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_01624,ECO:0000305|PubMed:11573087,ECO:0000305|PubMed:12072565;Dbxref=PMID:11573087,PMID:12072565 P0A006 UniProtKB Binding site 13 13 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11573087,ECO:0000269|PubMed:12072565,ECO:0000269|PubMed:12682056,ECO:0000269|PubMed:15159594,ECO:0000269|PubMed:16797027;Dbxref=PMID:11573087,PMID:12072565,PMID:12682056,PMID:15159594,PMID:16797027 P0A006 UniProtKB Binding site 36 36 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11573087,ECO:0000269|PubMed:12072565,ECO:0000269|PubMed:12682056,ECO:0000269|PubMed:15159594,ECO:0000269|PubMed:16797027;Dbxref=PMID:11573087,PMID:12072565,PMID:12682056,PMID:15159594,PMID:16797027 P0A006 UniProtKB Binding site 63 63 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11573087,ECO:0000269|PubMed:12072565,ECO:0000269|PubMed:12682056,ECO:0000269|PubMed:15159594,ECO:0000269|PubMed:16797027;Dbxref=PMID:11573087,PMID:12072565,PMID:12682056,PMID:15159594,PMID:16797027 P0A006 UniProtKB Binding site 65 65 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11573087,ECO:0000269|PubMed:12072565,ECO:0000269|PubMed:12682056,ECO:0000269|PubMed:15159594,ECO:0000269|PubMed:16797027;Dbxref=PMID:11573087,PMID:12072565,PMID:12682056,PMID:15159594,PMID:16797027 P0A006 UniProtKB Disulfide bond 10 82 . . . Note=Redox-active%3B alternate;Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305,ECO:0007744;evidence=ECO:0000255|HAMAP-Rule:MF_01624,ECO:0000305|PubMed:11573087,ECO:0000305|PubMed:12072565,ECO:0007744|PDB:1LK0;Dbxref=PMID:11573087,PMID:12072565 P0A006 UniProtKB Disulfide bond 82 89 . . . Note=Redox-active%3B alternate;Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000255|HAMAP-Rule:MF_01624,ECO:0000305|PubMed:10606519,ECO:0000305|PubMed:11573087,ECO:0000305|PubMed:12072565,ECO:0007744|PDB:1JFV,ECO:0007744|PDB:1LJU;Dbxref=PMID:10606519,PMID:11573087,PMID:12072565 P0A006 UniProtKB Natural variant 2 2 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. D->T P0A006 UniProtKB Natural variant 24 33 . . . Note=In strain: SW18. GKEILGEGWN->AKQILAKDWD P0A006 UniProtKB Natural variant 24 31 . . . Note=In strain: SW24 and SW1. GKEILGEG->AKQILADD P0A006 UniProtKB Natural variant 24 31 . . . Note=In strain: SW4. GKEILGEG->AKQILAED P0A006 UniProtKB Natural variant 56 56 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. D->G P0A006 UniProtKB Natural variant 65 65 . . . Note=In strain: SW24 and SW1. D->N P0A006 UniProtKB Natural variant 70 76 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. DILKQSD->NIIKNSN P0A006 UniProtKB Natural variant 87 87 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. N->V P0A006 UniProtKB Natural variant 91 91 . . . Note=In strain: SW4%2C SW24 and SW1. I->S P0A006 UniProtKB Natural variant 91 91 . . . Note=In strain: SW18. I->T P0A006 UniProtKB Natural variant 94 94 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. P->T P0A006 UniProtKB Natural variant 110 110 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. E->P P0A006 UniProtKB Natural variant 123 123 . . . Note=In strain: SW4%2C SW24 and SW1. L->I P0A006 UniProtKB Natural variant 123 123 . . . Note=In strain: SW18. L->V P0A006 UniProtKB Natural variant 127 127 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. K->N P0A006 UniProtKB Natural variant 130 130 . . . Note=In strain: SW18%2C SW4%2C SW24 and SW1. L->S P0A006 UniProtKB Mutagenesis 10 10 . . . Note=Loss of activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10606519;Dbxref=PMID:10606519 P0A006 UniProtKB Mutagenesis 10 10 . . . Note=Loss of activity%3B when associated with A-15. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10606519,ECO:0000269|PubMed:11573087;Dbxref=PMID:10606519,PMID:11573087 P0A006 UniProtKB Mutagenesis 13 13 . . . Note=Loss of K(+) stabilization over Na(+). N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682056;Dbxref=PMID:12682056 P0A006 UniProtKB Mutagenesis 15 15 . . . Note=2-fold decrease in affinity for arsenate. Does not affect affinity for pNPP. Loss of activity%3B when associated with S-10. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10606519,ECO:0000269|PubMed:11573087;Dbxref=PMID:10606519,PMID:11573087 P0A006 UniProtKB Mutagenesis 16 16 . . . Note=Loss of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12072565;Dbxref=PMID:12072565 P0A006 UniProtKB Mutagenesis 17 17 . . . Note=5-fold decrease in catalytic efficiency. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12072565;Dbxref=PMID:12072565 P0A006 UniProtKB Mutagenesis 21 21 . . . Note=Decreases the thermal stabilization effect of K(+). E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682056;Dbxref=PMID:12682056 P0A006 UniProtKB Mutagenesis 36 36 . . . Note=Strong impact on thermal stabilization. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682056;Dbxref=PMID:12682056 P0A006 UniProtKB Mutagenesis 62 62 . . . Note=Uncouples the sulfate effect from the potassium effect on the kinetics. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16797027;Dbxref=PMID:16797027 P0A006 UniProtKB Mutagenesis 65 65 . . . Note=Loss of K(+) stabilization over Na(+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682056;Dbxref=PMID:12682056 P0A006 UniProtKB Mutagenesis 82 82 . . . Note=Loss of activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10606519;Dbxref=PMID:10606519 P0A006 UniProtKB Mutagenesis 89 89 . . . Note=Loss of activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10606519;Dbxref=PMID:10606519 P0A006 UniProtKB Mutagenesis 89 89 . . . Note=Leads to a reductase locked in the C-10/C-82 intermediate form. Decrease in affinity for pNPP. C->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11573087,ECO:0000269|PubMed:12072565;Dbxref=PMID:11573087,PMID:12072565 P0A006 UniProtKB Mutagenesis 105 105 . . . Note=4-fold decrease in catalytic efficiency. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12072565;Dbxref=PMID:12072565 P0A006 UniProtKB Beta strand 4 15 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Helix 16 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Turn 29 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Beta strand 32 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Helix 46 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Helix 69 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Beta strand 76 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Helix 83 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Beta strand 96 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8 P0A006 UniProtKB Helix 111 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JF8