ID A0A081NFG7_9GAMM Unreviewed; 901 AA.
AC A0A081NFG7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KEQ17190.1};
GN ORFNames=GZ78_15215 {ECO:0000313|EMBL:KEQ17190.1};
OS Endozoicomonas numazuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1137799 {ECO:0000313|EMBL:KEQ17190.1, ECO:0000313|Proteomes:UP000028073};
RN [1] {ECO:0000313|EMBL:KEQ17190.1, ECO:0000313|Proteomes:UP000028073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25634 {ECO:0000313|EMBL:KEQ17190.1,
RC ECO:0000313|Proteomes:UP000028073};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEQ17190.1}.
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DR EMBL; JOKH01000003; KEQ17190.1; -; Genomic_DNA.
DR RefSeq; WP_051786266.1; NZ_JOKH01000003.1.
DR AlphaFoldDB; A0A081NFG7; -.
DR STRING; 1137799.GZ78_15215; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000028073; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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 GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-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; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; PS00551; MOLYBDOPTERIN_PROK_1; 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 Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028073}.
FT DOMAIN 12..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 901 AA; 98710 MW; 53AB0EE86F2D5788 CRC64;
MAGSINISNE HPKVIHTTCA YCGVGCGIKA TVTDKELHLV DIEGRKDHPA NLGRLCSKGS
ALGETVSLEN RLLTPFIDEQ RVGWDKALDE VANRLKATLD EYGPEAVALY GSGQLLTEDY
YVANKLMKGF IGTGNMDTNS RLCMASTVAG QKRAFGSDTV PGSYEDLELA DMVVLVGANT
AWCHPVLFQR IRAAKEQRPE MKVVVIDPRV TDTCDIADLH LPLKSGTDTA LFNKLFSYLQ
KHNKVDTAYV DQHTQGFEEA LKAAEKVGDF SAVAELCGVE KTALKQFCQW FADTDKVVTA
WSQGVNQSVA GTDKVNAIVN CHLITGRIGK PGTGPLSLTG QPNAMGGREV GGLANQLAAH
MEFANAEDID RVRRFWNAPN IARSPGKTAV DLFNAMDNGE IKFVWIMGTN PVVSMPDANT
VISALKKCPT VVVSDCIEKT DTSEFAHIRL PAAGWSEKDG TVTNSERRIS RQRALFDLSG
ESKPDWWIIS RVAEKVGFGE AFDYQSSADI FREHAALSAF ENNSQGRVRD FNIGAVASIS
DAEYEALEPF QWPLIKGHKA AQPHTRLFAD GGYFTETGRA TVVSTEFKVS YHQPNTDYPL
LLNTGRVRDH WHTMTRTALS PRLSQHMDEP FVEVHPDDAE KYGLADQALC RLSTAFDSIL
IRVTVTPSVG KGNVFMPMHW TRQNSKTGHC GVLVKSAVDP WSKQPGCKHT PASIEAVSLQ
QQAVLLSRQK QCFDRFDYGT EVKFQQGFRY ELAGQSIDTT ALDIIGSEKE RIDYTDPETG
SSRSAWFALG QLQALLIVGE TLSDSDRSWL QGAFDKEDIP FSERWRLLAG MPPQGEDTGK
VICACFGVGE KTICRAIEEE GFSDPAEVGQ SLKAGTNCGS CIPEIRKLIS QVEDLAINAA
S
//
