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Database: UniProt
Entry: C5AIL8_BURGB
LinkDB: C5AIL8_BURGB
Original site: C5AIL8_BURGB 
ID   C5AIL8_BURGB            Unreviewed;       776 AA.
AC   C5AIL8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Oxidoreductase alpha (Molybdopterin) subunit {ECO:0000313|EMBL:ACR31748.1};
GN   OrderedLocusNames=bglu_2g13880 {ECO:0000313|EMBL:ACR31748.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31748.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR31748.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR31748.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
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   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP001504; ACR31748.1; -; Genomic_DNA.
DR   RefSeq; WP_015877442.1; NC_012721.2.
DR   AlphaFoldDB; C5AIL8; -.
DR   STRING; 626418.bglu_2g13880; -.
DR   KEGG; bgl:bglu_2g13880; -.
DR   PATRIC; fig|626418.3.peg.1667; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_4; -.
DR   Proteomes; UP000002187; Chromosome 2.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT   DOMAIN          113..514
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          653..760
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   776 AA;  85015 MW;  54257AAAD50BC83E CRC64;
     MKKKAPIPRI EPYHHAAAGW GAVKQVAINL IKERVAGGNY RTLFKQNQPD GFDCPGCAWP
     DRQHASTFEF CENGVKAVAA EATSKRATPA FFAAHTVTAL LDQSDYELEQ HGRLTDPMVY
     DAASDRYVPI AWDDAFTLIA RHLKALDDPN RAAFYTSGRA SNEAAFLYQL MVRRFGTNNF
     PDCSNMCHEA TSRGLPASVG VGKGTVTLDD FEHADLLLIF GQNPATNHPR MLGELRECAK
     RGAKIVSINP LRERGLERFS DPQSPLEMLT MGSTRIATSF VQPTIGGDFA LIKGIAKRVL
     ELDDAAVLAG EPRVLDVAFI DAHGAGFDAF AADLRAESWA ALSAESGVSY QQIDSLARLY
     ASSERVIATW GMGITQHKHS VQTIHMLSNL MLMRGNIGRR GAGLCPVRGH SNVQGNRTVG
     IEEKPGAAFL DRLGQVYGFA PPRRHGYDVV ETIEALLDGR VNVFIGLGGN FAMATPDTPR
     TWEGLRRCAL TVHITTKLNR SHLIHGSDAL ILPTLGRTEI DLQNGVAQGV TVEDSMSMVH
     VSYGMNQPAS PNLLSETAIV ARMAMALFGP DDTVDWRGYL NDYARVRDAI EATLPGFENY
     NARIAQPGGF HLRVASRERE WLTPNGKANF IAHALPTDSP IHRARARHGE KLLTLMTTRS
     HDQYNTTIYA LDDRYRGVFG QRRVVFANRD DLAMLGLRAG ERVDLETVWH DGIERRAEGF
     LLVEYDIPRG CLGAYYPETN PLVPLDSTAD IANTPTSKSI PVLLHRSAAG AARAAA
//
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