ID A4ETM0_9RHOB Unreviewed; 536 AA.
AC A4ETM0;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Oxidoreductase, GMC family protein {ECO:0000313|EMBL:EBA17059.1};
GN ORFNames=RSK20926_08817 {ECO:0000313|EMBL:EBA17059.1};
OS Roseobacter sp. SK209-2-6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA17059.1, ECO:0000313|Proteomes:UP000005964};
RN [1] {ECO:0000313|EMBL:EBA17059.1, ECO:0000313|Proteomes:UP000005964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA17059.1,
RC ECO:0000313|Proteomes:UP000005964};
RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EBA17059.1}.
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DR EMBL; AAYC01000004; EBA17059.1; -; Genomic_DNA.
DR RefSeq; WP_008205767.1; NZ_AAYC01000004.1.
DR AlphaFoldDB; A4ETM0; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000005964; 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; 3.50.50.60; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000005964}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 259..273
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 536 AA; 58472 MW; B3491D2801FEDBEB CRC64;
MQFDYVIVGG GSAGATLASR LSEDPKTTVC LLEAGGKGDS ILVRAPAAVV AMLPGRPKIN
NWAFETVPQA GLNGRKGYQP RGKALGGSSA INAMLYVRGH AKDYDEWAEL GCRGWDWQGV
LPYFQKAENN ERGADEYHGA EGPLQVSNQK APRKITEAFV EAGESLQLRR SADFNRGENE
GIGHYQVTQF HAEKKNGERC SAAAAYLHPV MGRSNLKVIT KAHAKQILFE GKRATGVRYA
KGATDHEVKA AREVILCGGA FNSPQLLQLS GVGRPEDITP HGIKLLHDLP GVGQNLQDHL
DFTLAYKSRN RDNFGISLPG SLALLKHIAA WRKTGRSMIA TPFAEGAAFL KTESDLARPD
VQLHFVISIV DDHARKLHLG HGFSCHICVL RPKSRGTVTL NSADPLAAPR IDPNFLSEEE
DLQVLIRGTR MCRRIMQAEP LASYIKKELF IEGEPDDAAL ERHIRERADT IYHPVGTCKM
GQDEMSVVDP DLKVHGLEGL RVVDASVMPR LIGGNTNAPT IMIAEKAADL IRNKAV
//
