ID A0A0A0BSZ5_9CELL Unreviewed; 1250 AA.
AC A0A0A0BSZ5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=N868_13755 {ECO:0000313|EMBL:KGM10782.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM10782.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM10782.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM10782.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM10782.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM10782.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
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 -!- 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:KGM10782.1}.
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DR EMBL; AXCY01000039; KGM10782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0BSZ5; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000029839; 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: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 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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
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 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; PS00490; MOLYBDOPTERIN_PROK_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000029839}.
FT DOMAIN 68..132
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 137701 MW; 40BE7F6AE7B96AE7 CRC64;
MNPTTERTEG TGRADRPGRP GLDSPASDVL LRLGRHLRKG EVSYDLRTLH QAGGREADTF
YRDRWSHDKV VRSTHGVNCT GSCSWKVYVK DGIITWEAQQ TDYPSVGPDR PEYEPRGCPR
GAAFSWYTYS PTRVRYPYVR GVLLQMYREA KARTGDPVEA WASIVDDPEA SRRYKRARGK
GGLVRATWDE AVEIVAAAQV HTIRRYGPDR IAGFSPIPAM SMVSHGAGAR YHSLIGAPML
SFYDWYADLP VASPQVFGDQ TDVPESGDWW DAGYLIMWGS NIPVTRTPDA HWMAEARYRG
QKVVAVAPDY ADNVKFADEW LAAAPGTDGA LAMAMGHVVL REFFVDRQVP YFTDYVKRYT
DLPFLVRLDE TPDGVVPGKF LTASDLPGAE ARTENAEFKT VLLDAGTGAP VVPGGSLGFH
YGDDGAGRWN LDLGDVDPVL SIAEDRAAEG AVEVTLPRFD TLDGSAATVR RGVPVRRVGE
HLVTTVFDLM LAQYGVGRPG LPGQWPTGYD DPTGGCTPAW QEQFTGVPAA KAERIGREFA
ANAEESRGRS MIIMGAGTNH WFHSDTIYRS FLALTTLTGC QGVNGGGWAH YVGQEKCRPV
TGHGHYANAL DWSRPPRTMI QTAYWYLHTD QFRYDQFGAD TLASATPGAA RGQLSGRTTA
DVVALSARLG WMPSYPTFDR NPLDLADEVA ASGRSVAEHV PAELLAGRLR FAAEDPDAPE
NFPRVLTVWR ANLLGSSAKG NEYFLHHLLG TDSNLRATPT PPEARPRDVV WREEAPTGKL
DLLLALDFRM TSTTVYSDVV LPAATWYEKH DLNTTDMHPF VNSFSPAIAP PWQTRTDFDI
FHTLARRFSE LGAQHLGVRK DVVAVPLTHD TPDEMATPHG RVRDWKSGEC DPVPGRTMPK
LVVVERDYGA IAAKMASLGP LLDTLGTTTK GITYDVREEV ELLARKNGVV RGGGVADGRP
SLARDVHACE AILALSGTTN GRLAVQGFET LEKRTGQHMA DMAAEHEGKK VTFSDTQAAP
VTVITSPEWS GSEHGGRRYS PFTINVERLR PWHTLTGRQQ FFIDHDWMTE LGENLPVFRP
PLDMASLFDE PVIGETGALG VTVRYLTPHN KWSIHSEYQD NLFMLSLSRG GPTIWMSDVD
AAKVGVGDND WVEAVNRNGV VVARAVVSHR MPEGTVYMHH AQDRLIDVPL SETTGRRGGI
HNSLTRLLIK PSHLIGGYAQ LSYAFNYLGP TGNQRDEVTV IRRRSQEVTY
//
