ID A0A426GR46_9CAUL Unreviewed; 555 AA.
AC A0A426GR46;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:RRN66583.1};
GN ORFNames=EIK80_04705 {ECO:0000313|EMBL:RRN66583.1};
OS Caulobacter sp. 602-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN66583.1, ECO:0000313|Proteomes:UP000268773};
RN [1] {ECO:0000313|EMBL:RRN66583.1, ECO:0000313|Proteomes:UP000268773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=602-1 {ECO:0000313|EMBL:RRN66583.1,
RC ECO:0000313|Proteomes:UP000268773};
RA Gao J., Sun J.;
RT "The genome of Caulobacter sp 602-1.";
RL Submitted (NOV-2018) 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:RRN66583.1}.
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DR EMBL; RRYI01000001; RRN66583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426GR46; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000268773; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 555 AA; 60064 MW; 8F5CD91F30EA3B5A CRC64;
MASERYDYVI IGAGSAGCVL AARLTEDPGV KVLLLEAGGK NTSILVKMPA GVGELIKAKG
EQNWGFWTEA EPHLDNRKLW WPRGKGLGGS SAINGMIYIR GHARDYDQWR QMGLSGWSYE
EVLPYFKRSE THHAGGDAYH GDKGPLYVSK GESDSPFYST LIEAGRQAGH KTTKDFNGFQ
QEGFGPYDLT IRDGQRWSAA MAYLNQALAR PNLTVVTEAR TTRIIVEKGR AVGVDYVVGK
AAEKKTAHAD AEVLLSAGAV QSPHILQLSG IGAPDDLKAH GIAVVHESKG VGGNLQDHLD
VCVSWTAKNL KTAYSANKGL NKLGVGLGYM FFGKGLGRQQ FLESGAFLKS RPDLDRPDLQ
IHGVLAIMQD HGKVVVEKDG FTLHVCQLRP ESRGKIGLRS ADPFDDPTIL ANYLATDEDR
RAIREGVRIA RETVAQAAFD PYRDAEYAPG ADVRSDADLD AWIRAKAETI YHPVGTCRMG
VAGDPLAVVD DQLRVQGLQG LRVIDASVMP TLVGGNTNAP TIMIAERAAD LLRGRTLLAP
LDVPVFEDGR AVAAE
//
