ID F3Z0C4_DESAF Unreviewed; 730 AA.
AC F3Z0C4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:EGJ49826.1};
GN ORFNames=Desaf_1489 {ECO:0000313|EMBL:EGJ49826.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49826.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49826.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49826.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP003221; EGJ49826.1; -; Genomic_DNA.
DR RefSeq; WP_014259612.1; NC_016629.1.
DR AlphaFoldDB; F3Z0C4; -.
DR STRING; 690850.Desaf_1489; -.
DR KEGG; daf:Desaf_1489; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0051536; F:iron-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; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR CDD; cd02755; MopB_Thiosulfate-R-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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..730
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003308866"
FT DOMAIN 47..103
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 730 AA; 79945 MW; BFECC2EDC8DA7980 CRC64;
MTPNKARRIS RRGFLKAAGA VAAGLAAARP ETVAAVAGSP AATITEWESR FSACDMCFNR
CGLIARVENG VVRKLDPNPK FLKSRGMLCA RGNAGIAQLY DPDRLKHPLL RVGERGEGKW
KRISWDEALD LAAQRLQAIR KEHSPSGVLF MAGSDMQSSF VNRFAEVFGS FNVTSHESNC
LMSNTRAYLD TFGEVPFPDV LNSKYVLMAG ANRFEALVTP DSMDLMTAMR ERGCKLVVLD
PRFTKTAALA HEWWPIKPGT DMAFMLAVMH VITSENLYDK AWVAEKTYGI EQLTQHVKRY
DPRWAEGETG IPAADIARMA REMAAAAPQS MVYPGRRSSD YVNSTQIRRS FAMLNALLAN
WDRPGGLLGA REVGLGSGIP FSAPWYDENP FERADAGIAP LMIEHEGSYV LLREAVLKGE
PYPLKGFFSF KVNPLATAPD RAKSIEMMKA FDFSVVVDIA MSDTAWFADL VLPAPSYLER
MDPASALQGS SACACVVDRD PVVPAMFESR PVFDICKALA QRLELGEFFD FDMAAFRKAQ
LKDLPGAEKA LAEDGVYYNP SKVYGIYEGR IYKTKSQKIE FFNQRYADEG LDPMPVYSAP
KAVPDGMFRM VVGRSAVYTH SATNNALLRQ LEPDCLLWIN PKRADALGIK DGDAVIVQSA
VGKGQAKALV TEAIRADTAY MPTGFGALSK GLSLAHGNGA SMAGVLESNF DAISGNAAMH
ETFVTVTRKA
//
