ID A0A1G0T537_9BACT Unreviewed; 754 AA.
AC A0A1G0T537;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Nitrate reductase catalytic subunit {ECO:0000313|EMBL:OGU79665.1};
GN ORFNames=A2W11_09385 {ECO:0000313|EMBL:OGU79665.1};
OS Ignavibacteria bacterium RBG_16_35_7.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798434 {ECO:0000313|EMBL:OGU79665.1, ECO:0000313|Proteomes:UP000178403};
RN [1] {ECO:0000313|EMBL:OGU79665.1, ECO:0000313|Proteomes:UP000178403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OGU79665.1}.
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DR EMBL; MHAG01000203; OGU79665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0T537; -.
DR Proteomes; UP000178403; Unassembled WGS sequence.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR PIRSF; PIRSF000144; CbbBc; 2.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 40..96
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 754 AA; 83328 MW; FF3A4B076EF9932C CRC64;
MSISRRNFLK ASALTAAAAA IGVEPLHKSS VLAAAVQESV VWYKSVCRFC GVGCGVMLGV
KDGKPFGIKG DKECPVNKGL LCVKGFYLHR MITAKNRLLH PLVRKNGKLE KASWDEAMDL
VASRFKEILE KDGPNALAYY GSGQAQTEET YLAQRLFKGY IGTNNADGNP RLCMASAVGG
YTTSFGADEP IGTYKDIEHC NLFLIIGSNT AEAHPVIFDL LVQRKKDSPS CKIIFIDPRK
TPTNRIVDLH LQVKPGYDLA IMHAIARQLI KDGYTDEQFI KDSVNFSNGK DPITYDDYKA
FLEKYTPEYA AEQADINPAD IVKAARMFGE SPTAMTMWCM GVNQRVAGVF LNNLIHNIHL
LTGKLGKPGC DSFSLTGQPN ACGGVREAGG LCHILPGHRL VANEQHRKVV AEIWKTSPDK
IQPTPGKHTV AMFGAAAKGE IKGMYILCTN PAQSLPNLNK YIPGMKDTFL VVAESFYPTE
TSKIADVVLP VAFWGEKEGV YGCTERRSQH LAKALNPSGE SRWDGDVIVD LAKRMGYGKG
FEHFKGPEDV WSEYQKTTAG TDMDLSGATY DRLKKVRGLT WPVPDTSHPG TWHRFTEGDP
YFPKDKAGNR RMYFYAKPDG KAVIFARPDK GPEEPVSAEY PVVLTTGRIL EQWHTMTMTG
QIPELVRANP VPYAELNPDD AKLWGIKNRD KVKITTRRGL LTVEAKVIDR TRKGTIFIPW
HWPESLTNIL TIDAVDPGSF EPEYKVAACQ VAKA
//
