ID B4X037_9GAMM Unreviewed; 886 AA.
AC B4X037;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Molybdopterin oxidoreductase Fe4S4 domain family {ECO:0000313|EMBL:EDX89980.1};
GN ORFNames=ADG881_2082 {ECO:0000313|EMBL:EDX89980.1};
OS Alcanivorax sp. DG881.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=236097 {ECO:0000313|EMBL:EDX89980.1, ECO:0000313|Proteomes:UP000003954};
RN [1] {ECO:0000313|EMBL:EDX89980.1, ECO:0000313|Proteomes:UP000003954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG881 {ECO:0000313|EMBL:EDX89980.1,
RC ECO:0000313|Proteomes:UP000003954};
RA Bolch C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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; DS989915; EDX89980.1; -; Genomic_DNA.
DR RefSeq; WP_007150388.1; NZ_DS989915.1.
DR AlphaFoldDB; B4X037; -.
DR STRING; 236097.ADG881_2082; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_000422_13_4_6; -.
DR Proteomes; UP000003954; 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 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.
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 16..65
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|SMART:SM00926"
SQ SEQUENCE 886 AA; 96273 MW; F8FAC5D3144423AF CRC64;
MSVEAKIQET EPKNAPLSTC TTCPYCGVGC GIRTDGVTLK GDTQHPANAG RLCVKGSSVL
ETLGDQDRLL NPEVDGEVVS WDQALDEVAG RFRRIVDEHG PDAVAFYVSG QLLTEDYYVA
NKLMKGYIGS ANIDTNSRLC MSSAVVAHKR AFGEDVVPGC YEDLELADLV ILTGSNTAWA
HPIVYQRIVA AKQARPDMKV VVIDPRRTAT CDLADLHLAI RPGQDVPLFN GLLTWLDDNK
ALDQAYIDAH TEGFQATLET ARRQGNDWEA LAAKMGVSKV DLTTFYHWFA ACERTVTVFS
QGVNQARNGS DQGNAIINAH LATGRVGKSG ASPFSITGQP NAMGGREVGG LANQLAVHLD
IDNPAHHAAV ADFWQAPALA TKNGLTAVEL FEAVSSGEVK AVWIMATNPV DSLPEADKVR
QALMACDTVV VSDCVASGDT LACADIRLPA LGWGEKSGMV TNSERCVSRQ RPFVPAPGQA
KADWWIITEV AQRMGFADAF PYQHEHDIFA EYSALTAVAG QFGKRLDLTG AADLSADQYA
QWQPQHWPLN GDPRCYADGQ FSTPSGRARF VSCENPPARQ IGDAFPIILN SGRIRDQWHT
MTRTGRAGRL FAHLSEPFAA LHPQDIERYR LQEGGFVRLT SRVGDALVRV TRDTGQRPGT
AFMPMHWTDQ FSRRARVDAL VPARLDPHSG QPAFKHTPVN VSDWQPRWHG WLFTAASPPA
VEYWARVPVD AFLQAGQVQR YRLAGDADLT EQQLHDWLPQ AAQWLALNDP ATGHYRRAAL
DKDGHLLAWL AIGETLPVCD VDWLADCFAV EADIQHMAIL AGQPADAGPD LGPVICSCFQ
VRQKTIEGVV EEGADSVEAI GKGCQAGTNC GSCIPELRGL LETCTS
//
