ID A0A0M2USW0_9BACT Unreviewed; 910 AA.
AC A0A0M2USW0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=BROFUL_03229 {ECO:0000313|EMBL:KKO18081.1};
OS Candidatus Brocadia fulgida.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO18081.1, ECO:0000313|Proteomes:UP000034954};
RN [1] {ECO:0000313|EMBL:KKO18081.1, ECO:0000313|Proteomes:UP000034954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KKO18081.1};
RX PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA Keltjens J.T., Jetten M.S.;
RT "Identification of the type II cytochrome c maturation pathway in anammox
RT bacteria by comparative genomics.";
RL BMC Microbiol. 13:265-265(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001854};
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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:KKO18081.1}.
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DR EMBL; LAQJ01000295; KKO18081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2USW0; -.
DR PATRIC; fig|380242.3.peg.3975; -.
DR Proteomes; UP000034954; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 5.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-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 NCBIfam; TIGR03479; DMSO_red_II_alp; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034954}.
FT DOMAIN 54..118
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 910 AA; 103252 MW; 4EE8CB99A2973BD1 CRC64;
MSQDESIRAS EVLAGQGEKV LLPALDLLEH ISEPIGKYPY QGWESLYREQ LDYDYFGRTT
HSVNCTGSCT WKVYVKNNIA FKEEQYADYP DINASLPTYN PRGCQKGANY KEYVYGPQRL
KYPLMRAGAR GEGKWRKASW EEATSYIANK MVNAISNYGP DTVTFYSANP AKFAITYTGG
VRLANLIGAV VCSFYDWVSD LPPGEPITWG VQTDSCEAAD WFNSKYIIVW GSNILETRIP
DAHFLTEARM HGTRIVAIFP EYNPTSIHAD MYVPVKPGTD CALALCMANV IMNEKLYDET
YIKQYTDMPI LVRMDSGKFL RENDMVQDGS PDKFYVWDLS LDRPALVPGT KGTLNTIGWT
LNLGSMNPAL EGTFTINTLS GEIKVTTVFS LLKQKLATYD PPHVSVITGV DADLVTQIAR
EFAKTKPARI IGGAGTNHHY HNDLMSRSHI LLAAMTGNVG IQGGGFDYYV GQERFWPEDG
FVKLAYPLGR SKQRFQPTTL WTYVHAHIAS EVNNLWPRPM IDYIRESVSN GWMPLYPEGT
LDNGKSPKVL IIWGANYLNQ AKGFESILTN LWPKLDLIVD IDFRMNTTGL YADVILPAAS
MFEKWDLSVT DLHSYINPFT PIIEPQMDSK TDWQIWQLLA KALQDTKFSF TDILPGGITL
TRDFSTLVND FTENGSLASD KSAGQCILDN AVETKGMTMD GINQQPRRFV ATHEERTSDI
KEGVAYYGFQ RMYELKRPLS TLTGRQQFYI DHQWFLDFGE QLPAYKPPVD EDKYPLRWNT
PHGRWSIHSV WRDAKYQLRL QRGRPIVHLN PAEAQARSLA DNDAIEIYND HGKIVAQLCI
SQRIPAGMAH MYHGWERYNF EKGGFQSPTT IRMKPTQLVG GYGQLEFRFN YWGPTASQRD
TRVNIRKYIS
//