ID E1VMR6_9GAMM Unreviewed; 939 AA.
AC E1VMR6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Assimilatory nitrate reductase {ECO:0000313|EMBL:CBL46108.1};
GN Name=narA {ECO:0000313|EMBL:CBL46108.1};
GN ORFNames=HDN1F_25250 {ECO:0000313|EMBL:CBL46108.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL46108.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL46108.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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; FP929140; CBL46108.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VMR6; -.
DR STRING; 83406.HDN1F_25250; -.
DR KEGG; gpb:HDN1F_25250; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000002677; 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:UP000002677}.
FT DOMAIN 26..83
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"
SQ SEQUENCE 939 AA; 102850 MW; FE048F58BFF481BA CRC64;
MTVITFHPAP TLQNSDTNER TNHSDTTVTH TTCPYCGTGC GITASTDHVD LSLQVTGNSG
HPSNHGRLCS KGSSLASTLR PDGRLLHPKI HGIRASWEQA ISFVAKQLSD IIATHGPDAV
AFYVSGQLLT EDYYVANKLM KGFIGSANID TNSRLCMSTA VAGHKRAFGE DVVPGCYEDL
ELADLVVLAG SNTAWCHPVL FQRIKAAKAQ KPDMKVVVID PRATSTTEIA DLHLALRPGS
DVLLFNGLLG WLADHNVVDT DYISRHTGHF EQALRSAWQD ADTLEQVAEG CDLEIDKLTT
FYRWFAETPR TTTLFSQGIN QSSSGTDKVN AIINCHLATG RIGKPGASPI SLTGQPNAMG
GREVGGLANQ LAAHMELTPD NIARVKRFWN AENMAQHPGL KALDLFKAIG EGKVKAVWIM
GTNPVVSLPD ADRVKMALEN CPLVIASDCI ERTDTNDLAH VLLPAMGWGE KDGTVTNSVR
CISRQRRLPA AGLSATHLLT TGEARQDWRI LRDVAHAMGF ARHFDYAKSA DVFREHAALS
AFENEGSHKR LFNLSGLQTL SDEDYDQLSP LQWPVTEEIT STIRDPENSL RLFGDGVFCT
EDGKARFVAV QWQPPANATD TTWPLVLNTG RIRDQWHTMT RTGLSASLNQ HKPEPFVELH
SDTALRYHIQ SGHLVRISTR WGNMLARATT DAGIRRGDVF VPIHWNDQFA RNARVGALVN
PATDRHSGQP EGKHTPCQIE HWTPDWTGFV FSRQELSLPT SQWASKIRGE HFFRYEIAGE
GPLPDLDTLS LITGVTSTHE PALLFEDQSA GRFRWAHLVD GELESCVFVE KGDSDRIRNA
DRRWLASLFS KATLDPLDRK ALLSGKSPAG VEDAGRTVCA CYGVGEKTIC NAIARHQLKT
AAEVGQHLKA GTNCGSCVAE IKALIEKQSE PQPTTLTLP
//