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Database: UniProt
Entry: A0A1C1YYQ2_9RHIZ
LinkDB: A0A1C1YYQ2_9RHIZ
Original site: A0A1C1YYQ2_9RHIZ 
ID   A0A1C1YYQ2_9RHIZ        Unreviewed;       567 AA.
AC   A0A1C1YYQ2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE            Short=CDH {ECO:0000256|HAMAP-Rule:MF_00750};
DE            Short=CHD {ECO:0000256|HAMAP-Rule:MF_00750};
DE            EC=1.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00750};
DE   AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE            Short=BADH {ECO:0000256|HAMAP-Rule:MF_00750};
DE            EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00750};
GN   Name=betA {ECO:0000256|HAMAP-Rule:MF_00750};
GN   ORFNames=AWJ14_18325 {ECO:0000313|EMBL:OCW58536.1};
OS   Hoeflea olei.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Hoeflea.
OX   NCBI_TaxID=1480615 {ECO:0000313|EMBL:OCW58536.1, ECO:0000313|Proteomes:UP000094795};
RN   [1] {ECO:0000313|EMBL:OCW58536.1, ECO:0000313|Proteomes:UP000094795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC234 {ECO:0000313|EMBL:OCW58536.1,
RC   ECO:0000313|Proteomes:UP000094795};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant
CC       glycine betaine. Catalyzes the oxidation of choline to betaine
CC       aldehyde and betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|SAAS:SAAS00321133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde;
CC         Xref=Rhea:RHEA:17433, ChEBI:CHEBI:13193, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00750,
CC         ECO:0000256|RuleBase:RU003969, ECO:0000256|SAAS:SAAS01117340};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00750,
CC         ECO:0000256|SAAS:SAAS01117337};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00750, ECO:0000256|PIRSR:PIRSR000137-2,
CC         ECO:0000256|SAAS:SAAS01080756};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine aldehyde from choline (cytochrome c
CC       reductase route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00750,
CC       ECO:0000256|RuleBase:RU003969, ECO:0000256|SAAS:SAAS00321105}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|RuleBase:RU003968,
CC       ECO:0000256|SAAS:SAAS01080758}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OCW58536.1}.
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DR   EMBL; LQZT01000006; OCW58536.1; -; Genomic_DNA.
DR   RefSeq; WP_066176557.1; NZ_LQZT01000006.1.
DR   EnsemblBacteria; OCW58536; OCW58536; AWJ14_18325.
DR   BioCyc; GCF_001703635:AWJ14_RS06050-MONOMER; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000094795; Unassembled WGS sequence.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 4.10.450.10; -; 1.
DR   HAMAP; MF_00750; Choline_dehydrogen; 1.
DR   InterPro; IPR011533; BetA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01810; betA; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000094795};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|PIRSR:PIRSR000137-2,
KW   ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080750};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00750,
KW   ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080744};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|SAAS:SAAS00321145};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00750,
KW   ECO:0000256|SAAS:SAAS01080751};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094795}.
FT   DOMAIN       80    103       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      256    270       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND       4     33       FAD. {ECO:0000256|HAMAP-Rule:MF_00750}.
FT   NP_BIND      90     93       FAD. {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   ACT_SITE    470    470       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00750}.
FT   BINDING      82     82       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
SQ   SEQUENCE   567 AA;  61673 MW;  E05DBC0FBE826EB7 CRC64;
     MQADFVIVGA GSAGSAMAAR LSEDGKHSVI VIEHGGSDFG PFIQMPAALS YPMNMGIYDW
     GYTTEPEPHL GNRRLAAPRG KVIGGSSSIN GMVFVRGHAE DFNHWAEQGA TGWSFADVLP
     YFKRMETSHQ NGGVGGEAGW RGTDGPLHVQ RGTLKNPLFR AFIEAGRQAG YGVTEDYNGS
     RQEGFGQMEQ TIHNGQRWST AEAYLKPALK RQNVSLVRGL ARRVVIENHR ATGVEIEAHG
     AIQVVQARRE VIVAASAFNS PKLLMLSGIG PGAHLAEHGI AVIADRPGVG SNLQDHLEVY
     IQQECIQPIT LYSKLNLVSK ALIGAQWLFL RQGLGTSNQF EACAFVRSAA GVPYPDIQFH
     FLPGAIRYDG KAAAPMHGFQ AHVGPMRSPS RGAVRLRSGD AKAAPVIRFN YMNCEEDWRD
     FRRAVRITRE VFSQPAFDPY RGQEIQPGAH VQSDEEIDGF IREHAESAYH PCGTCRMGRA
     DDPNAVVDPE TRVIGVEGLR VADSSIFPRV TNGNLNGPSI MTGEKAADHI LGRTPLAPSN
     LEPWLNPHWR ETDRLAAPDS PPQAAAS
//
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