ID A9G3T2_SORC5 Unreviewed; 631 AA.
AC A9G3T2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN OrderedLocusNames=sce5632 {ECO:0000313|EMBL:CAN95795.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN95795.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN95795.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM746676; CAN95795.1; -; Genomic_DNA.
DR RefSeq; WP_012238260.1; NC_010162.1.
DR AlphaFoldDB; A9G3T2; -.
DR STRING; 448385.sce5632; -.
DR KEGG; scl:sce5632; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_4_1_7; -.
DR OrthoDB; 9785276at2; -.
DR BioCyc; SCEL448385:SCE_RS28945-MONOMER; -.
DR Proteomes; UP000002139; 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; 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:SF213; DEHYDROGENASE, PUTATIVE-RELATED; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT DOMAIN 341..355
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 631 AA; 70474 MW; A52E460C6C49F37E CRC64;
MIGEQGARGD YEYVVVGSGA GGGTVAARLA EAGHTVVLLE AGGDPRALSG GDAFQPDKNR
LPDDYDVPVF HSLASENNAI KWDFFVRHYA NEEQQRRDPK YRETWQGNPT RGVLYPRAGT
LGGCTAHNAM ILVYPQNDDW DHIAELTGDA SWRADKMRGY FELLENCHHR PFHRFLSMFG
FNPTRHGWSG WLQTEKAIPK VALGDRDLVR FLLESAYRAS HAVTTPIERL RSLFQGKADP
NDWRSVRVNA TGVRYLPLTT RNHQRSGPRE RVLDVARRYP DRLKIELNAL VTRVLFDEQN
RAVGVEYQKG ARLYRAGANP AEENGERRTL RASREVILAG GAFNTPQLLM LSGVGPRDEL
ERHGIAVRVD LRGVGKNLQD RYEVGVVNRM SFDHWDVLKG ARYSPGDPQY RQWATHRAGV
YTTNGSVLAV INRSVPERPL PDLFCFALLG RFMGYFPGYS ADGPKHLNYL TWAILKAHTE
NRAGEVTLRS ADPRDTPEIN FRYFEEGGDT RGEDLESMVA GIKFVRTLTA PLKKEGLIAE
EELPGDHVQS DDDLKGFVRD NAWGHHASCS CAIGPREQDG VLTSDFRVHG TQGLRVVDAS
VFPRIPGFFI VSAVMMIAEK AADVILADAR G
//
