ID F8GY90_CUPNN Unreviewed; 563 AA.
AC F8GY90;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Choline dehydrogenase BetA {ECO:0000313|EMBL:AEI82831.1};
DE EC=1.1.99.1 {ECO:0000313|EMBL:AEI82831.1};
GN Name=betA {ECO:0000313|EMBL:AEI82831.1};
GN OrderedLocusNames=CNE_BB2p00120 {ECO:0000313|EMBL:AEI82831.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OG Plasmid pBB2 {ECO:0000313|EMBL:AEI82831.1,
OG ECO:0000313|Proteomes:UP000006798}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI82831.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI82831.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RC PLASMID=pBB2 {ECO:0000313|EMBL:AEI82831.1,
RC ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
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}.
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DR EMBL; CP002880; AEI82831.1; -; Genomic_DNA.
DR RefSeq; WP_013954114.1; NC_015724.1.
DR AlphaFoldDB; F8GY90; -.
DR KEGG; cnc:CNE_BB2p00120; -.
DR HOGENOM; CLU_002865_7_1_4; -.
DR Proteomes; UP000006798; Plasmid pBB2.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 2.
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 FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000313|EMBL:AEI82831.1};
KW Plasmid {ECO:0000313|EMBL:AEI82831.1}.
FT DOMAIN 4..304
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 371..557
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 563 AA; 60324 MW; 340FE0848748A3AC CRC64;
MTFYDDLIVG AGAAGSVLAN RLSADPQRRV LLLEAGRDIR PGDEPADIRS IFPLSTFNPA
YMWPDTLVHW GRANGTAPSF FPQGRLLGGT SQIMGMFALR GRPEDYDDWA AMGAAGWGWD
DVLPFFRKLE SDHDFSGTMH GCDGPVPIRR EPQAQWSPLS ARLHQVAAAR GFSHVADMNA
DFGDGYGTLP ISRYPDKRGS AGICYLDAAV RARSNLTVQA GATVSRLLLE RRDGALHCTG
VACTDAQGQV RQIRARRVLL AAGALRTPAL LLRAGIGPGD ELTRLGIAPQ LERKGVGRNL
QNHAILYVVA FLARAGREPG GVRPACATTM RWSSAQHGGT PGDMGMYIRS WLSWHALGHR
MASLAPVLNK PWSRGSVTLS AQAPQAQTVV EFDLLSDPRD LARITSAFRF TASLFGELGG
ICGTPYVLSD ARNLSRLMRY NEPTSANAVR AAAAARLIDA MPGFGQRMVA KLSKMTPAAE
VLRSDDALAD YARRSISGTG HVSGTCRMGA ASDPLAVVDP HGRVHGMQGL YVADASVMPT
VPSANTHLPT IMVAEKIAQG LLV
//