ID A0A136LTH9_9BACT Unreviewed; 535 AA.
AC A0A136LTH9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KXK24925.1};
GN ORFNames=UZ12_BCD005001791 {ECO:0000313|EMBL:KXK24925.1};
OS Bacteroidetes bacterium OLB12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK24925.1, ECO:0000313|Proteomes:UP000070129};
RN [1] {ECO:0000313|EMBL:KXK24925.1, ECO:0000313|Proteomes:UP000070129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK24925.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
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}.
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:KXK24925.1}.
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DR EMBL; LNFR01000066; KXK24925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LTH9; -.
DR STRING; 1619897.UZ12_BCD005001791; -.
DR PATRIC; fig|1619897.3.peg.1952; -.
DR Proteomes; UP000070129; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 535 AA; 59021 MW; 6E9460A80AE9FB1F CRC64;
MTFDYIIVGA GSAGCVLANR LTENPAITVL LLEAGPKNTK LETTIPGGYM KLHRSSVDWN
CYWTTPQPFL QNRKLYHPRG KVLGGCSTTN AMAYVRGHAA DYNHWASLGN TGWSYDDVLP
YFIKSEHNEQ FQNRYHGQTG LLNVTHGLRH KTPLAQAFID ACAQTGIVRN DDFNGAQQEG
AGLMQFTIKG ARRCSTADAF LKPVLLRDNL TVYTGVHVKQ ILIEKDEATG VEYFIRDACC
EKVFARKEVI LCGGAFASPQ LLMLSGVGPK EVLEKHNIEV KKELPGVGQN LQDHLFFAVS
SLCNKPISNN HWMPWYRQIQ SLVQYALFKT GPLTLGPLEA CAFIKSDTSQ PKPDLQFQFT
PTHVGNDYTT DLFDLTTFPH TDGYTILPTQ VNPKSRGYLT LASADPFAAP VIDPNYLSHE
TDRTTLVKGA RIALQILEAD AFTPYRTKTH CPAQRDSDEA LLNHIQRSAE CVYHPVGTCK
MGNDALAVVN DQLQVYGIGN LRVVDASIMP TLTSGNTNAP VIMIAEKAGD LIKGN
//
