ID A0A1U9JRI8_9NEIS Unreviewed; 899 AA.
AC A0A1U9JRI8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:AQR66712.1};
GN ORFNames=BXU06_05660 {ECO:0000313|EMBL:AQR66712.1};
OS Aquaspirillum sp. LM1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Aquaspirillum.
OX NCBI_TaxID=1938604 {ECO:0000313|EMBL:AQR66712.1, ECO:0000313|Proteomes:UP000188659};
RN [1] {ECO:0000313|EMBL:AQR66712.1, ECO:0000313|Proteomes:UP000188659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM1 {ECO:0000313|EMBL:AQR66712.1,
RC ECO:0000313|Proteomes:UP000188659};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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}.
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DR EMBL; CP019509; AQR66712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9JRI8; -.
DR STRING; 1938604.BXU06_05660; -.
DR KEGG; aql:BXU06_05660; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000188659; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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 GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-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; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 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.
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 Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000188659}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 899 AA; 95851 MW; BC7ECC9D22DFC309 CRC64;
MMMTVKSTCC YCGTGCGIEI DVCDGQVCGV RGDPDHPANF GRLCTKGLTL PHTLHTASRL
AEPRLRPGRT GLGEAVSWDI ALDAVSDRLA AIIAEHGPES VAFYLSGQML TEDYYVYNKL
ARGLIGTPHV DTNSRLCMSS AVTGYKLALG ADAPPCSYED FDHADCVLIA GSNMAYAHPV
LFRRLEAART ANPNMKLIVV DPRRTDTAAS ADLHLAIQPG TDVALFNGML HALIWDDRLD
RGFISEHTEG FAELRHAVRE YTPKMAADIC GISEDALLTA ARWFGEAGAA LSLWCMGLNQ
SAHGTDKNLA LINLHLATGQ IGRPGAGPFS LTGQPNAMGG REVGGLATAL SGHRDPANPQ
HRAEVAALWG VDALPATPGK TAIPMFDAIA AGQIKALWIV CTNPAHSMPD ANQVREALAA
CEFVIVQDAY ADTDSIDYAD VLLPAAGWAE KDGTVTNSER RISRVRRAVA APGSARADWD
IGIDAARRLA ARLGRGGHLF PYAGPDEVFA EHCLTTVGRD LDIGGLSYAV LEAEGPQQWP
RPAGASQGAA RLYTDHRFAT DTGRARFHLT PYHGVAEAVT ARYPFHLLTG RLRDQWHGMS
RSGRVPALFA HTAEAVLSMH AGDMARRGLS EGELVRMSNQ HGDWVLPVQA DSGMLSGQLF
VPMHWSSGFV ASAGSNALTA GKMDKRSFQP ELKHAAVRLD KIELAWQCAA VSACGDPVSL
LTALRPLLAE CRFASATLLD GDTPAVRVRF AHPTLPSAHF LAQLDRALGL EGEAGVQQLF
SDPRRGIHKL AVWQGSRLRG VRLAGECCAL GWLGERIVSG GDMGELRALV FAPQASPAGL
TRRARMVCHC AKVDETAIYQ ALAKGASADS LRETLGCGSG CGSCMPEVRR MAAAVSKAA
//
