ID A0A0F3H0R5_9BACT Unreviewed; 717 AA.
AC A0A0F3H0R5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=NarB, nitrate reductase {ECO:0000313|EMBL:KJU86523.1};
GN ORFNames=MBAV_001281 {ECO:0000313|EMBL:KJU86523.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU86523.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU86523.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU86523.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) 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:KJU86523.1}.
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DR EMBL; LACI01000559; KJU86523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3H0R5; -.
DR PATRIC; fig|29290.4.peg.1702; -.
DR Proteomes; UP000033423; 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; 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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000033423}.
FT DOMAIN 3..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 717 AA; 78826 MW; 69B77EA200E23447 CRC64;
MSVIWHKSTC PYCGFGCGIM VGVDGGKVVK TTGMKGHPTN DGRLCVFAET LPAALYAPDR
LTHPMIRRQG SLVKVTWQEA IEHVAKTLLD IIRRHGPDAV AFYGGASKLT EEYYLISKLM
RACIGTNNIE CSTRLCMAST AAGFLSTIGA DAPPACYADI EEADLFFIAG NNMAVTVPVL
FQRVRAAKKA NGVKVIVVDP RKTETAAIAD IHLQLRPGTD VALNNALAHV LLRDGFVDEY
KVQHYTSSLC DLKDFLKDYT PEFVSQITCC PPTQIVEAAH AIGRSKAMLT FWFQGYNHSS
QAVFKNNTLH NLSLLTDNFC RVGAGPISIT GESNALGCRF VGALSNLLPG MRLVTNATHR
QEVADFWGIP VEKINPLPGR SIIDIITGLH SGEVKALFVA TTNPAASLPH TRWVQEGLAK
AQMLVVADIF HPTETTMLAN VILPAAQWAE KTGTFVSSER RIELVEKLVQ PPGDALPDYE
IIWLIARQMG FEKEFPYNSP EEVFEEWKGL TRGRLCDSNG VTYQRLREGV GPQLPCPTPE
HPGSARLFSG MQFVRPDGRA ALLARKYIEP AETPDAEYPF MLITGRLAGQ FNTRTRTGRI
DRLNRLTANS FVEINTEDAL ALGITEGDVV EVTSRRGNVV GDVLLSQRIL PGTVFIPCHF
GGALGGDDNR LVNRVTNPVY DIHSKQPEFK ISAVKIVRDG CCIDKTYLNM FKYYHSE
//
