ID D2R7G4_PIRSD Unreviewed; 555 AA.
AC D2R7G4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ADB15660.1};
GN OrderedLocusNames=Psta_0975 {ECO:0000313|EMBL:ADB15660.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15660.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB15660.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
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; CP001848; ADB15660.1; -; Genomic_DNA.
DR RefSeq; WP_012909925.1; NC_013720.1.
DR AlphaFoldDB; D2R7G4; -.
DR STRING; 530564.Psta_0975; -.
DR KEGG; psl:Psta_0975; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_0; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000001887; Chromosome.
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; 2.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
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 Pfam; PF00732; GMC_oxred_N; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 12..59
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 60..324
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 405..546
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 555 AA; 60905 MW; B9B24A099C2DE751 CRC64;
MKSASTSSGE FDVVIVGSGA TGGVAAMELT SFGLKTLVLE AGPKLDATQV VGRGGINQLK
RVYRHLVSNP QPIQKMHPGY WECSPDLFVS DAENPYSHPA DKPYHWIRGR HVGGRSLTWG
GVTLRLSDYE FKPAQQDGEG VDWPIGHDDL APYYAKLETY FQVHGSREAL PQLPDGEFLP
PSEMTPAELM LKASLAEHAP DRRMIICRGI GSSRTHRPSR EQPWPMLSSP GTSLRTAMAT
GLCELRDNAV VRHVVCDPHT RLASGVEFVD RLTKQTHCVR AKYVVLCAST IETNRILLLS
LREQQPGGLV DTSGLLGTHL TDHIATATNV LLPRVPQAQR PFELFGSDSV LIPRFRNLGK
SDAPFLRGYG LWGGIQRFAP LPDFLRKGEP GATGFLAGHG EVIARAENRV TLHPSRVDAC
GIPIPHIEFA WSTNEKLMVA DMQQQIRDLI AMAGGHCLDM ADIYRVPPPF GAHIARMEQL
MTCSTPGLYV HELGGARMGT TEENSVVGPH NQWWSCPNLL VTDGACWPTS GWQNPTLTEM
AITARACHYL ATQLR
//
