ID T0GXS8_9SPHN Unreviewed; 550 AA.
AC T0GXS8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EQB05507.1};
GN ORFNames=L288_12745 {ECO:0000313|EMBL:EQB05507.1};
OS Sphingobium quisquiliarum P25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB05507.1, ECO:0000313|Proteomes:UP000015525};
RN [1] {ECO:0000313|EMBL:EQB05507.1, ECO:0000313|Proteomes:UP000015525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P25 {ECO:0000313|EMBL:EQB05507.1,
RC ECO:0000313|Proteomes:UP000015525};
RX PubMed=24029763;
RA Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a Novel
RT Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an HCH
RT Dumpsite.";
RL Genome Announc. 1:e00717-13(2013).
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:EQB05507.1}.
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DR EMBL; ATHO01000109; EQB05507.1; -; Genomic_DNA.
DR RefSeq; WP_021238767.1; NZ_ATHO01000109.1.
DR AlphaFoldDB; T0GXS8; -.
DR PATRIC; fig|1329909.3.peg.2465; -.
DR Proteomes; UP000015525; 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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 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;
FT DOMAIN 110..331
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 420..536
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 59941 MW; B081065F58E7D6B5 CRC64;
MSSGAVMPLE PRAKDGRAPD VFVPGGWTPM GEHRDTEAVD FAIVGTGAGG GTLACRLAEA
GFSVVAFDAG AYWRPLEDFA SDERHQSKLY WNDDRIVEGA NPLKLGANNS GKSVGGSTVH
YAMVALRFRP EWFKSRSLLG YGADWPIDWR EMWSYYAEVE QALAIAGPVT YPWGPKRPRY
PRRAHPLNAP AALLARGAEA LGIGWSETPI ATLSSPRGKA RPCVYRGMCT IGCSTNAKQS
VLNTWLPRAL AAGAEIRDLA MVGRVETDAR GMATGVHYQR GGEWRFQRAR NVVVAGYAIE
TPRLLLNSAS PLFPDGLANS SGLVGRNLMV QLNQAVWGQM EQEVRSYKAP PSLALTEHWN
YEDRGKDYHG GWCYMSQGPL PIGWAQTVAG GRRMWGQSLV DEMNRANHSV GLKMVGEVMP
SPDNRVTLAN EVDAYGLPIP RISFSYGDNE HAMLAHALPF MEQALEAVGA HELWREEEDT
CHLNGTARMG DDPATSVVNA DCRSWDIPNL WICDGSVFPT VGGANPSLTI QAIACRTADR
IAAMGKRGEL
//
