ID A0A0D7KCI9_9BURK Unreviewed; 1266 AA.
AC A0A0D7KCI9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KJA10863.1};
GN Name=narZ {ECO:0000313|EMBL:KJA10863.1};
GN ORFNames=RP29_08410 {ECO:0000313|EMBL:KJA10863.1};
OS Acidovorax temperans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA10863.1, ECO:0000313|Proteomes:UP000032566};
RN [1] {ECO:0000313|EMBL:KJA10863.1, ECO:0000313|Proteomes:UP000032566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY4 {ECO:0000313|EMBL:KJA10863.1,
RC ECO:0000313|Proteomes:UP000032566};
RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT "Isolation of bacteria from lake water.";
RL Submitted (DEC-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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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:KJA10863.1}.
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DR EMBL; JXYQ01000023; KJA10863.1; -; Genomic_DNA.
DR RefSeq; WP_044397307.1; NZ_JXYQ01000023.1.
DR AlphaFoldDB; A0A0D7KCI9; -.
DR STRING; 80878.RP29_08410; -.
DR PATRIC; fig|80878.5.peg.1205; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000032566; Unassembled WGS sequence.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
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; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 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 Pfam; PF14710; Nitr_red_alph_N; 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; PS00490; MOLYBDOPTERIN_PROK_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000032566}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1266 AA; 141921 MW; 611DA39E5AFC8E62 CRC64;
MSHFLDRLTH FSAPTESFSG QHGLTNGEDR TWEDAYRDRW AHDKIVRSTH GVNCTGSCSW
KIYVKGGIVT WETQQTDYPR TRPDLPNHEP RGCSRGASYS WYLYSANRVK YPMVRARLLK
HWRAALAVAR SPVDAWASIV ENDTARREWQ KQRGLGGFVR STWDEVNQMI AAANVYTIKK
HGPDRIIGFS PIPAMSMISY AAGSRYLSLI GGVSMSFYDW YCDLPPSSPQ TWGEQTDVPE
SADWYNSNFI IAWGSNVPQT RTPDAHFLTE VRYKGTKVVS ITPDYSEVAK LGDLWMHPKQ
GTDAAVAMAM GHVILKEFYF KDGGKGRSSY FDDYARRYTD LPLLVVLKEK TLPDGRKAMV
PDRYVRASDF PNKLDQSNNP DWKTVGYDEL GQVTLPNGSI GFRWGTDGRP DQGLWNLENK
DARTGNTVKL KLSVIEDGEQ PHDVADVAFP YFGGVHAPNF TANDQGGDVM VRRVPVSHLE
LDGHEVQGRV MVATVFDLLA ANYGIDRGLP GEEPGGSYDA DRPFTPAWQE KITGVPREQI
ITVARQFADN AHKTHGKSMV IIGAAMNHWY HSDMNYRGII NMLMLCGCIG QSGGGWAHYV
GQEKLRPQTG WTALAFALDW IRPPRQMNST SFFYAHTDQW RYEKLGMEEI LSPLADARAY
HGAQIDYNVR AERMGWLPSA PQLKTNPMQV AKDAAAAGMD AKDYVVKSLK DGTLTMSCED
PDHPSNWPRN MFVWRSNILG SSGKGHEYFL KHLLGTTHGV QGKDLGKDEA KPEEVQWHAN
APEGKLDLLV TLDFRMSTTC LYSDIVLPTA TWYEKNDLNT SDMHPFIHPL STAVDPAWQA
KSDWEIYKGF AKAVSEVSVG HLGVEKDVVL TPIMHDTAGE MAQPYGVSDW KKGECELIPG
KTAPQITVVE RDYPNLYKRF TALGPLMEKA GNGGKGIGWN TQTEVGQLGD LNGRVKEEGV
TKGMPRIVTD IDATEVVMML APETNGHVAC KAWEALGKQT GRDHVHLALH REDEKIRFRD
IQAQPRKIIS SPTWSGLESE KVSYNAGYTN VHEYIPWRTL TGRQQFYQDH PWMRDFGEGF
VSYRPPVHLK TLEEVEGKKP NGNREIALNF ITPHQKWGIH STYSDNLMML TLNRGGSVVW
LSEDDAKSAG IVDNDWVELF NANGAIAARA VVSQRVNPGM VMMYHSQEKI INTPGSEITG
TRGGIHNSVT RIVLKPTHMI GGYAQYSYGF NYYGTIGTNR DEFVLVRKMD RVDWLDDEVS
DTGAHA
//
