ID B2JJM1_PARP8 Unreviewed; 564 AA.
AC B2JJM1;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ACC72219.1};
GN OrderedLocusNames=Bphy_3050 {ECO:0000313|EMBL:ACC72219.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72219.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP001043; ACC72219.1; -; Genomic_DNA.
DR RefSeq; WP_012402396.1; NZ_CADFGH010000011.1.
DR AlphaFoldDB; B2JJM1; -.
DR STRING; 391038.Bphy_3050; -.
DR KEGG; bph:Bphy_3050; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_4; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000001192; Chromosome 1.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT DOMAIN 262..276
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 564 AA; 62342 MW; 74DF8FF2B075A7E7 CRC64;
MSTTTRKVEG EFDYIIIGAG TAGCVLANRL TEDSDVTVLL LEAGGKDDYH WIHVPVGYLY
CIGNPRTDWL YKTQAEPGLN GRALSYPRGR VLGGCSSING MIYMRGQRED YDEWARVTND
SSWAWDAVLP VFRRSEDHHG GANEFHGVGG QWRVEKQRLK WKILEMFAQA ATETGIPATD
DFNRGDNTGV GYFDVNQKRG IRWNASKAFL RPAMQRPNLT VITGAHTQRV VFEGKRCVGV
EYRGDHVEYI AKARLEVIMS SGAVNSPQLL ELSGVGNGAR LQKLGIEVVN DLRGVGENLQ
DHLQLRMAYK VHGVRTLNTA SAHWWGKMAI GLQYLLMQSG PMSMSPSQLG AFAKSDTDDR
TLTRPDLEYH VQPLSLDKFG EPLHRFNAFT ASVCHLRPTS RGSVHIESRD PHVAPLIAPN
YLSTDYDRHV AANALRLTRR IAAAPALQRY RPEEILPGIQ FQTEEELQLA AGNVGTTIFH
PVGTCRMGTA DDPGAVVDSR LRVVGVEGLR VVDASVMPTI TSGNTNSPTL MIAERASDMI
RVDRRARAHS LSIETRVALP MSVA
//
