ID B1TAG6_9BURK Unreviewed; 759 AA.
AC B1TAG6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Oxidoreductase alpha (Molybdopterin) subunit {ECO:0000313|EMBL:EDT39437.1};
GN ORFNames=BamMEX5DRAFT_4782 {ECO:0000313|EMBL:EDT39437.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT39437.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT39437.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT39437.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:EDT39437.1}.
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DR EMBL; ABLK01000191; EDT39437.1; -; Genomic_DNA.
DR RefSeq; WP_006760594.1; NZ_ABLK01000191.1.
DR AlphaFoldDB; B1TAG6; -.
DR PATRIC; fig|396597.7.peg.2946; -.
DR Proteomes; UP000004814; Unassembled WGS sequence.
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; 2.40.40.20; -; 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}.
FT DOMAIN 113..484
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 642..750
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 759 AA; 83012 MW; F9CE6C0D26544F34 CRC64;
MTDRREVPGI RKYDGPAGGW GALRATAEAV RTQMETIEAP IVLMRTNQPD GFDCPGCAWP
DKEHKSTFQF CENGAKAVTW EATTKRVTPE FFAANPVSSL LRMSDYELEN MGRLTHPLVY
DRATDTFRAV EWDDAFARIG EVLRALPPEQ VEFYTSGRAS NEAAYLYQLF ARELGTNNFP
DCSNMCHEPT SVGLPQSIGI GKGTVSLEDF DHCELIISIG HNPGTNHPRM MGTLHECARR
NVPIIVFNPL RERALERFAD PQDMIEMASF GSTRIASTYY QVDAGGDAAA LKGIMKALLQ
LEAERGNVLD RDFIAQHTSG FDAFSADLEA TSWDDIERAS GLSQAQLEQV ALAYAKSNAT
IVTYGMGVTQ HNKGTATVRL IADLLLMRGN IGKPGAGVCP LRGHSNVQGN RTVGITEKPS
AEFLQKIEDV CGFKPPAQHG HDAVQAMQAM IDGQAKALLC LGGNFAVALP DPEQSFPAMA
KLDLSVHLGT KLNRSHLLVA KETYILPVLG RTELDMQASG RQSITVEDSM SMVHASAGKL
KPASDQLRSE PAIVAGIAHA TLPASKVAWL DLIADYDRIR DLIDRTVAGF EAFNERIRTP
GGFRLPLPPT ERVWPTATGK AMFSIYKGVK EDADVLGAEQ VLRLITLRSH DQYNTTIYGL
DDRYRGVFGR RDVLFMNAAD LAKYGLEHGD LVDIETATTS GRTLRLEKIT AIEYDIAPGS
VGAYYPEANV LVPLDYIDKE SGTPSYKSVP VRVARSAVV
//
