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Database: UniProt
Entry: A0A1I3HEE9_9RHOB
LinkDB: A0A1I3HEE9_9RHOB
Original site: A0A1I3HEE9_9RHOB 
ID   A0A1I3HEE9_9RHOB        Unreviewed;       863 AA.
AC   A0A1I3HEE9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Assimilatory nitrate reductase (NADH) alpha subunit apoprotein {ECO:0000313|EMBL:SFI34106.1};
GN   ORFNames=SAMN04488095_0562 {ECO:0000313|EMBL:SFI34106.1};
OS   Jannaschia pohangensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=390807 {ECO:0000313|EMBL:SFI34106.1, ECO:0000313|Proteomes:UP000199110};
RN   [1] {ECO:0000313|EMBL:SFI34106.1, ECO:0000313|Proteomes:UP000199110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19073 {ECO:0000313|EMBL:SFI34106.1,
RC   ECO:0000313|Proteomes:UP000199110};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FORA01000001; SFI34106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3HEE9; -.
DR   STRING; 390807.SAMN04488095_0562; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000199110; Unassembled WGS sequence.
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:InterPro.
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:UP000199110}.
FT   DOMAIN          1..56
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   863 AA;  90749 MW;  58926E9D0A7A32AA CRC64;
     MNETRTTCPY CGVGCGVLLR QGPEGVSVRG DPDHPANFGR LCSKGSALAE TLTSEGRLLQ
     PRVDGADVSW DVALSRVADG FRTTLERHGP GSVAFYLSGQ LLTEDYYVAN KLMKGFMGSA
     NIDTNSRLCM ASTVAGHRRA FGSDTVPGTY EDLDEADLVV LVGSNLAWCH PVLFQRLVAA
     KAARGTKVVV VDPRRTATCD AADLHLALRG GSDTSLFNGL LAYLHANGHV DHTYVGAHVS
     GLDAAVAMAQ RDLSTTGLSA EDLAGFHALW ARSERVVTVF SQGVNQSTGG TDKVNAILNC
     HLATGRIGRP GCGPLSVTGQ PNAMGGREVG GLANMLAAHL DLEDPVHRSA VGRFWDAPAV
     ADRPGLKAID MFRAVRSGQI KALWIACTNP VASMPEADLV AEAIRTCDLS VVSDMYATTD
     TARCAQIVLP ALGWAEKDGT VTNSDRTISR QRGVVAAPGS ARADWDIFAE VGRRMGWREA
     FSYASPAEVF REHAALSGIA GRLGRDFDIS DLSGLDDRGY AALAPTRWPV SGARQGGRFF
     GAGGFFTPDG RGRMIPVATP EETASQPRYP FRLNTGRIRD QWHTMTRSAL TPRLSRHLAE
     PFLELHPADA VTLGLRAADI AQVQSPLGRA LLRVLVTDRV APGAPFAPMH WTAEFASAGR
     VDALIPGAVD PVSGQPDLKA ARVAISPFPA VWYGFAVSRS KPAPDAAYWA RSRIAGGWAV
     EMAGDVALVD WAGRAAAMFG LTTSPQTVTD RVSGQVRLAF FEDGLLHAAL FVSPGPVAVE
     RAHVAGLLGQ IAPDVLSGRS GAGRLDPGPV VCSCLGVGRN TIVAAAEAGM DVEACTGAGS
     NCGSCKPEIA ALIAGLAVRA AAE
//
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