ID A0A2S8SS79_9BACT Unreviewed; 718 AA.
AC A0A2S8SS79;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:PQV63661.1};
GN ORFNames=B1R32_110127 {ECO:0000313|EMBL:PQV63661.1};
OS Abditibacterium utsteinense.
OC Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC Abditibacteriaceae; Abditibacterium.
OX NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV63661.1, ECO:0000313|Proteomes:UP000237684};
RN [1] {ECO:0000313|EMBL:PQV63661.1, ECO:0000313|Proteomes:UP000237684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV63661.1,
RC ECO:0000313|Proteomes:UP000237684};
RX PubMed=29475572;
RA Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL Syst. Appl. Microbiol. 0:0-0(2018).
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:PQV63661.1}.
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DR EMBL; NIGF01000010; PQV63661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8SS79; -.
DR InParanoid; A0A2S8SS79; -.
DR Proteomes; UP000237684; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000237684}.
FT DOMAIN 327..508
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 595..710
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 718 AA; 78566 MW; 1F7DE2425A416634 CRC64;
MESYFDKLLA SPAVSDSTRK VYKARASHEP PPPQFFDAVD FATLIGVCQS LADVDLGARI
ASQIDHRLQV GTGNGWRFAD LPEDGLAIHL FLKALREADF DFETSDKSAI LESAKSGELE
TLPPNWAARR FFSDFLGEVL ETYASHPETQ AKMGYAGFAD KPGWTQIGLN EKQAREPDAA
TGEISLELEP FPNRETEWEG IAPQKMTGMK RYDLEEEVDA LVIGTGAGGG PLLARLAQNG
QKVVALEAGK WHDPRDFATD ERAQNFLFWL DERLSAGKNA VAFGANNSGI GVGGSTIHYT
AYTPRVLPDD FSIKTDFGVG HDWPITWQEI AEYYDEIEHF IGVSGPNPYP WGPARKRPYP
LAPLPINGAG QLMQRGCDAL GIRHSPAPNA ALSAPHYVLG VGWRAACSNR GFCQAGCSTG
GKSSIDVTYI PLAVAHGAEI RPETFVTKIE KSNGKITGVV YVENGVEKRQ KCKNLFLCAG
AIETPRLLLL NELANGSGQV GKNFMAHPGM QVWGTFDEDV RPYKGIPGAV ISQDTHRPKD
ADFVGGYLLQ SIGVMPVTYA SQYARGQMKF GEEMREHLQK YNHIAGINIL GDCLPYEHNF
LELSDELDGR GLPKPKLHFT AGESENKMDA HAEKIMRGIF EAAGARQMWS FQRHAHVIGT
AMMGTDPQKS VVNPDGRSHE IPNLYICDNS VFPSGLSVNP ALTIMALSLR TADKFLRG
//