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Database: UniProt
Entry: K8P615_9BRAD
LinkDB: K8P615_9BRAD
Original site: K8P615_9BRAD 
ID   K8P615_9BRAD            Unreviewed;       901 AA.
AC   K8P615;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN   ORFNames=HMPREF9695_01872 {ECO:0000313|EMBL:EKS38032.1};
OS   Afipia broomeae ATCC 49717.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=883078 {ECO:0000313|EMBL:EKS38032.1, ECO:0000313|Proteomes:UP000001096};
RN   [1] {ECO:0000313|EMBL:EKS38032.1, ECO:0000313|Proteomes:UP000001096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49717 {ECO:0000313|EMBL:EKS38032.1,
RC   ECO:0000313|Proteomes:UP000001096};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Afipia broomeae ATCC 49717.";
RL   Submitted (APR-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   -!- 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:EKS38032.1}.
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DR   EMBL; AGWX01000003; EKS38032.1; -; Genomic_DNA.
DR   RefSeq; WP_006020592.1; NZ_KB375282.1.
DR   AlphaFoldDB; K8P615; -.
DR   PATRIC; fig|883078.3.peg.1921; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_4_5; -.
DR   Proteomes; UP000001096; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001096}.
FT   DOMAIN          8..64
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   901 AA;  96083 MW;  96418536626DF216 CRC64;
     MTNVDPSVAP TKTTCPYCGV GCGVIATPDG KGGATIAGDP EHPANFGRLC SKGSALGETL
     GLGERLLHPM IRCSNGKFEE VAWTDALDHV ANRLQHIIAK YGPDSVGFYL SGQLLTEDYY
     VANKLMKGFI GTANVDTNSR LCMSSSVAGH RRAFGSDTVP GCYEDLDQAD LLVLVGSNAA
     WCHPVLFQRM IANKQQRGAR IVVIDPRQTE TSGDADLFLG LKPGTDTALF SGLLTYLADS
     GALDHSYIDE HTSGFAEGLA KARSIAGSVA ATALATGLAE TDVATFFQMF AKTPRVVTLY
     SQGVNQSAQG TDKVNAIINC HLATGRIGKP GASPFSLTGQ PNAMGGREVG GLANQLAAHM
     SFTPPDIDRV RRFWKAPHIA THEGLKAVQM FQAIGRGEIK ALWVMGTNPA VSLPNADAVR
     AAMRKLDLLV ISENVQSNDS INSGAHVLLP AHAWGEKSGT VTNSERRISR QRAFLTPPGQ
     AKPDWWIMSE VAERLGYGAA FAYHSAADIF REHAELSAFE NGGSRDFDIG AMASVADDEF
     DLMPPFMWPM PKGGSEAAPR FFAEGRYYTS DRKGHFIAPD VPMLRGAISE ARPLRLNTGR
     IRDQWHTMTR TGLSPRLGQH LPEPYVEIHP ADAAQADVVD GGYARLATDL GQCILKVVVS
     ERQQRGMLFA PIHWSQENSA SGRVGALVAP FTDPFSGQPE NKATPVAIES VTFGQRGFVL
     SRRLMSFPKD VGWSRVAVTG GYGYLIASNL DVAAWRTFLS PQGEAGHIAE YEDAAHGVYR
     AAQFSGDRLE ACVFIGPAKD IPSWDAVKTA FAAETISDEQ RRLLLSGKSA DGVANDGPVV
     CACFGVGRNA ICGAIAEGSR TAAEIGAKLK AGTNCGSCIP ELKRLIAQTG VAQPMEASAA
     S
//
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