ID A2BQC9_PROMS Unreviewed; 546 AA.
AC A2BQC9;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Glucose-methanol-choline (GMC) oxidoreductase:NAD binding site {ECO:0000313|EMBL:ABM69990.1};
GN OrderedLocusNames=A9601_07041 {ECO:0000313|EMBL:ABM69990.1};
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=146891 {ECO:0000313|EMBL:ABM69990.1, ECO:0000313|Proteomes:UP000002590};
RN [1] {ECO:0000313|EMBL:ABM69990.1, ECO:0000313|Proteomes:UP000002590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601 {ECO:0000313|EMBL:ABM69990.1,
RC ECO:0000313|Proteomes:UP000002590};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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}.
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DR EMBL; CP000551; ABM69990.1; -; Genomic_DNA.
DR RefSeq; WP_011818152.1; NC_008816.1.
DR AlphaFoldDB; A2BQC9; -.
DR STRING; 146891.A9601_07041; -.
DR KEGG; pmb:A9601_07041; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_3; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000002590; Chromosome.
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; 2.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 7..41
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 398..539
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 546 AA; 60891 MW; CDCD37FE671323C8 CRC64;
MDISPYDAIV VGSGATGGIA ALTLAEQGIK VLVIEAGPQV KRHEASNDEP KSTFKRLSGV
LTKKHANQCQ HPGYWKNNPD LYSNELKHPY DFPTKKPFLW TQGKQYGGRS LTWGGITLRL
SSEDFHPAKK DGFGPNWPIS YDELSPHYDF IENFCGIYGR KDDIKEVPNG KYIGEIPLTE
NENVFGNKVK SKLNYPFIQS RGFDRNSSVK EKKWPKSSSL GSSLKKALDT GNVQIISNYL
VESFEINKAT ELASKLTIVN LENGQKEVLN CDLIFLCAST ISTLRILLNS EYKTNSSGFK
DNSGKLGKYL MDHISICRFF SVPKTKNSDK PVDNPPDLSG AGSFFIPFGS NLPEIDDINF
HRGYGIWGAI DRLGIPKFLQ KDTNTSIGFL IAHGEVLPRE KNSVSLSRKT DEWGIPIPFI
EFEWSKNELN MAKHMENTIR KSITAANGEI KNINELINIP LGSLFTKNLI ALSDSPPPPG
YYIHEVGGAP MGIDEENSVV DKFNRLWRCK NVLVLDGACW PTSSWQSPTL TMMALSRRAC
LNIKKT
//
