ID J1S1S0_9ACTN Unreviewed; 815 AA.
AC J1S1S0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:QTZ91655.1};
GN ORFNames=SU9_009310 {ECO:0000313|EMBL:QTZ91655.1}, SU9_22175
GN {ECO:0000313|EMBL:EJJ04757.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ04757.1};
RN [1] {ECO:0000313|EMBL:EJJ04757.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ04757.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ91655.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ91655.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; AJGV01000132; EJJ04757.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ91655.1; -; Genomic_DNA.
DR RefSeq; WP_006605951.1; NZ_CP072931.1.
DR AlphaFoldDB; J1S1S0; -.
DR STRING; 1160718.SU9_22175; -.
DR KEGG; sauh:SU9_009310; -.
DR PATRIC; fig|1160718.3.peg.4486; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_11; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000009036; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009036}.
FT DOMAIN 42..98
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 88194 MW; EFD94EB7BFC046BF CRC64;
METSTDRIAE PWGSRSAYGP GQPWPVRVDA HFAPGVRPAD VERWVPSASL LHSNGDAMEI
AVLSGRIVGV RGRAVDRVNR GRLGPKDLFG WQANASPDRL TRPLVREGGR LVECDWPTAM
GRVASRSQQL LTERGPGSVG FYTSGQLFLE EYYTLTVLAR AGIGTHHLDG NTRLCTATAG
EALKETFGTD GQPGSYTDID HADTLALFGH NVAETQTVLW MRILDRLEGP QPPRLICVDP
RPTPVARRAT VHLPLRGGTN VALLNALLHE ILRTGRIDRD YLAAHTVGFE GLQAQVAACT
PQWAAGICDV PARLICEAAE ILGSAERLVS TVLQGVYQSH QATAAAVQVN NLHLVRGMLG
RPGAGVLQMN GQPTAQNTRE CGANGDLPGF RNWQNEEHIA DLARVWNVTP DRIPHDKPPT
PAMEMFRYAE QGSIRMLWIS GTNPAVSLPE LHRIRSLLAQ DRLFVVVQDL YLTETAQLAD
VVLPAATWGE KTGTFTNADR TVHLSEKAVD PPGQARPDLD IFLDYAARMD FRDKAGAPLV
AWHDAPSAFE AWQRCSAGRP CDYTGLSYDR LRETGGIQWP CNDQAPHGTE RLYTDGITWA
DPDLCESYGK DLETGAPADS AAYRSLNPQG KAVIRSAAYL PPPEDTSPDF PLQLNTGRTL
YHFHTRTKTG RTPQLDAAAP DVWAELSAAE AAAHALGEGD LIEVTTPRGA LRARLRITAM
RDGMVFVPFH YGYWDTPDGP PPEGAGRAAN ETTPTDWDPA SQQPLFKTGA ARISLVTRSD
GTPAPAPTIT ASAPASPGSL PPTTGGVEAY ATYDG
//
