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Database: UniProt
Entry: L8JIZ7_9GAMM
LinkDB: L8JIZ7_9GAMM
Original site: L8JIZ7_9GAMM 
ID   L8JIZ7_9GAMM            Unreviewed;       857 AA.
AC   L8JIZ7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Assimilatory nitrate reductase large subunit {ECO:0000313|EMBL:ELR67427.1};
GN   ORFNames=C942_01356 {ECO:0000313|EMBL:ELR67427.1};
OS   Photobacterium marinum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR67427.1, ECO:0000313|Proteomes:UP000011134};
RN   [1] {ECO:0000313|EMBL:ELR67427.1, ECO:0000313|Proteomes:UP000011134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK15 {ECO:0000313|EMBL:ELR67427.1,
RC   ECO:0000313|Proteomes:UP000011134};
RA   Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT   "Genome Assembly of Photobacterium sp. AK15.";
RL   Submitted (DEC-2012) 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   -!- 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:ELR67427.1}.
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DR   EMBL; AMZO01000002; ELR67427.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8JIZ7; -.
DR   PATRIC; fig|1056511.3.peg.428; -.
DR   Proteomes; UP000011134; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0042597; C:periplasmic space; 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; 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   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; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
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   Periplasm {ECO:0000256|ARBA:ARBA00022764}.
FT   DOMAIN          13..437
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          546..656
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   DOMAIN          800..849
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   857 AA;  94994 MW;  D8766F956AF20972 CRC64;
     MALGETVIHQ GRLLKPSIEG NNCNWDQALD YVADQFSEII REHGPQAVAF YVSGQLLTED
     YYVANKLMKG FIGSSNIDTN SRLCMSSSVA GHKRAFGADC VPGCYEDLEL ADLIILTGSN
     LAWCHPVLYQ RVKAAKQARP QLKIIVIDPR TTASCEIADL HLAIKPGTDV ALFNGLLCYM
     AQHGKLNQDY IASHTEGVKL ALSSARTDAE ELLKLAQKTE LSPQQLTAFF QHFADTENIV
     TVYSQGVNQS THGCDKVNSI INCHLATGRI GKPGCGPFSV TGQPNAMGGR EVGGLANVLA
     AHMDFGNDSH HQLISEFWQT DKLTKAPGLK AIEMFDAIDQ GKIKAVWIMA TNPAVSLPDS
     KKINRALTKC PIVVVSDCMA DTDTTRHASV LLPVQGWSEK SGTVTNSERR ISRQRRLLPT
     PGEGRPDWWI ISQVAKRMGF THAFNYRHEA EIFSEYCKMT GLGNHGQNRR QLNLSGFANL
     TAKEYHQLTP VQWPVISNQD FTTNEETQHN KRLFADGVFS TPSGKAQFIA VHSQPPASRT
     TVDYPLLLNT GRIRDQWHTM TRSGLAPRLS EHSPEPFISV SPEDASAYGL SHHQLAQISS
     PLGSATLHVN ITNDVRQGEL FAPIHWSNTN TSAAKICTLI YPHTDTLSGQ PEFKCTPVTI
     KRFNYRSEAV LLSTDSSEFE PELHKYEYWS KQRVANGYLF RIASLLPPKE LMLQLRHYCY
     RQNGRQLNFS NEAKEHYRFA AISHHQEQQQ LNCYFWVAGK LQHQELDWLH AIVGENADDT
     VARSLLSGSA EGRLRAGKNV CACKKVGKNT ICQAIREHQL DSVEQISTHT QAGTGCGSCI
     GEIQQLLSEQ QAKSPAP
//
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