ID L0GZA9_9GAMM Unreviewed; 624 AA.
AC L0GZA9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Choline dehydrogenase-like flavoprotein {ECO:0000313|EMBL:AGA92088.1};
GN ORFNames=Thimo_3422 {ECO:0000313|EMBL:AGA92088.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA92088.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA92088.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA92088.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP003051; AGA92088.1; -; Genomic_DNA.
DR RefSeq; WP_015282215.1; NC_019940.1.
DR AlphaFoldDB; L0GZA9; -.
DR STRING; 765912.Thimo_3422; -.
DR KEGG; tmb:Thimo_3422; -.
DR PATRIC; fig|765912.4.peg.3350; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_4_1_6; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000010816; 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 Pfam; PF13450; NAD_binding_8; 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 Reference proteome {ECO:0000313|Proteomes:UP000010816}.
FT DOMAIN 338..352
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 624 AA; 70079 MW; 8802802A5DC6B865 CRC64;
MSTENGFEYV VVGSGAGGGT VAARLAEAGR RVLLLEAGGD PIRLQGGDSA YPDAERLPED
YRVPAFHPFA SENQAMRWDF FVRHYGDEER QRRDPAYRET FGGKRVDGVL YPRAGTLGGC
TAHNAMIMVY PHNADWDEIA ELTGDASWKA DHMRGYFQRL ENCHHRLASY RWLAKIGVDP
TRHGFNGWLR TEKAIPKEVV GDEALVQVIA KSAIEALDEV GQPIDRVKWA VESQLDPNDW
RLVKDNAVGL RYPPLTTHRH ERMGTRERIL DVARRYPERL RIELDALATR VLFDDQQRAV
GVEYIKGTRQ YGAFQPPNAA DGEVRRVTAS REVVLAGGAF NTPQLLMLSG IGPKDHLAEH
GIETRVDLPG VGTNLQDRYE VGVVSRMKGD WEVLEGARFA EGDRQYREWD HLRQGVYTTN
GAVLAVIKRS RPERPLPDLF CFALLGNFRG YFPGYSKLFA AERQNYLTWA VLKAHTENRA
GVVRLRSADP RDTPHIDFRY FDEGSDSAGE DLDSVVDGVK FVRSLAHRYR HLIDEEELPG
KDVQTDDEIR QFVKDRAWGH HASCTCPIGA RDGGGVVDSR FRVHGTQGLR IVDASVFPRI
PGFFIVSAIY MIGEKAADLM LQDA
//
