ID A0A0T2QDW0_9SPHN Unreviewed; 535 AA.
AC A0A0T2QDW0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KRA82941.1};
GN ORFNames=ASD76_02320 {ECO:0000313|EMBL:KRA82941.1};
OS Altererythrobacter sp. Root672.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA82941.1, ECO:0000313|Proteomes:UP000051125};
RN [1] {ECO:0000313|EMBL:KRA82941.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA82941.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA82941.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA82941.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU003968}.
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:KRA82941.1}.
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DR EMBL; LMHH01000001; KRA82941.1; -; Genomic_DNA.
DR RefSeq; WP_055917920.1; NZ_LMHH01000001.1.
DR AlphaFoldDB; A0A0T2QDW0; -.
DR STRING; 1736584.ASD76_02320; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000051125; Unassembled WGS sequence.
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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; PS00623; GMC_OXRED_1; 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 ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000051125}.
FT DOMAIN 81..104
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 251..265
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 535 AA; 56704 MW; 79D54243C51CB454 CRC64;
MGREPDLIVV GGGSAGLACA TRLAEGGLRV LLVEAGKDHK DPRLAIPALM SGVVHKPDFD
WCYSAEPDPS VGGRPDVWPA GKRLGGGSSI NGMMFIRGHK WDFDHWAELG ATGWDYASVL
PYFRRLEHNE RGTDEWRGQG GPIHVSEVRS RYEVTDEWIE AAEQAGIPRS KDLNGEVGEG
VDMIQLSQRN GLRCSTAAGY LRNRPPGLEL LLEAQVLKIE VENGRATGVT IRRGGEVRTL
TARHGVVLSA GALNTPRLLM LSGIGPAGEL QQHGVAVVRD LPGVGQNLQE HPGCHLVNAV
SAHTLNNDAH GFAGVRQVLE LAFARSGALT TGIGHAQAFV KSREGLPAPN LQLAFSAFAF
EVTPKGNLAL AKDAAVSTFV AVMRPKSRGQ VRLRSGDPDA APLIEHRLLG EEDDAAQLVE
GLEIARQIMA QPAIAPHVKA EIRPGAAADS REALRGYVGA ATLPMFHPVG TAKMGAASDP
LAVTGPDCAV RGVQGLWVVD ASIMPTIPQG NTNATSIMIG ERASNLVLAG VREHT
//
