ID A0A1X4N9I2_9PROT Unreviewed; 906 AA.
AC A0A1X4N9I2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:OSQ43044.1};
GN ORFNames=THS27_11605 {ECO:0000313|EMBL:OSQ43044.1};
OS Thalassospira sp. MCCC 1A01428.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ43044.1, ECO:0000313|Proteomes:UP000193740};
RN [1] {ECO:0000313|EMBL:OSQ43044.1, ECO:0000313|Proteomes:UP000193740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ43044.1,
RC ECO:0000313|Proteomes:UP000193740};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL Submitted (MAR-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 -!- 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}.
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:OSQ43044.1}.
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DR EMBL; JFJZ01000012; OSQ43044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4N9I2; -.
DR STRING; 1470575.THS27_11605; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000193740; Unassembled WGS sequence.
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}.
FT DOMAIN 2..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 906 AA; 98519 MW; 205F1690F14FC7CD CRC64;
MQGEVKTTCP YCGVGCGLIV SPTRDGWAVG GDPDHPANRG RICSKGAALI DTVTAETKRD
FRLLSPEIDG KIADWKTATN ETARRLRQTI DQHGPKSVAF YVSGQLLTED YYVANKLIKG
FIGSPHIDTN SRLCMASTVV GHKRAFGADV VPGCYEDLEI ADLVILTGSN LAWCHPVLNQ
RLRAAKEKRG TRIVVIDPRK TASCDIADLH LPIKPGSDVA LFNGLLAWLE QNGQCDPTYL
SRHVSGYEDA IAAARAECPD IASTAKKCGL DDPVKTDQTA SGLTKLETFF QWFAKFERTV
TVFSQGVNQS SSGSDKVNAI INNHLATGRV GKPGASPFSV TGQPNAMGGR EVGGLANQLA
AHMDPNNVND VNRVKRFWKS DILKAGEGYK AVDMFRAIET GEIRAVWIMA TNPAVSLPDA
SRVRLALSRC PLVIVSDTVN DTDTLRYAHI KLPAAGWGEK SGTVTNSERR ISRQRPFRNQ
QGDAKPDWWI ISQVATAMGY GKAFKYRDPA EIFAEHAALS EFENDGVRAF DIGIWRKTKK
SAYDAMEPFQ WPASRKHQPK DGAHRLYGNG IFTTSNGRAR MLAVQHKLPL SQTSTDFPLI
GNSGRYRDQW HTMTRTGTAA RLSAHRPEPL LEVNPVDARR YGLCDGGLAR IKSLQGTALM
RVSISNAQMP GEVFMPMHWN DVYSSAGGIG RLATANVDPY SGQPETKYIP VSIEPFTALW
QGLLFSNAPV DLSHLPYWVA ASGPGCMIYE IASDKPCLFK SMLTAAANIG SDNTVEQIIE
YSDGKKGIHR YARLVGECIT GALFVGPKRP TLGRDWISTL LGNAAISTSE RNALLAGRMP
DATAVNDRLI CSCFSVGLTA ITRAIHTQNA MTPADIGRLL QAGTGCRSCL PEISELVSNT
LPRAAE
//
