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Database: UniProt
Entry: A0A1H1T565_9PSED
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ID   A0A1H1T565_9PSED        Unreviewed;       567 AA.
AC   A0A1H1T565;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=SAMN05216598_1946 {ECO:0000313|EMBL:SDS55291.1};
OS   Pseudomonas asplenii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=53407 {ECO:0000313|EMBL:SDS55291.1, ECO:0000313|Proteomes:UP000199524};
RN   [1] {ECO:0000313|Proteomes:UP000199524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23835 {ECO:0000313|Proteomes:UP000199524};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC       betaine. Catalyzes the oxidation of choline to betaine aldehyde and
CC       betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000256|HAMAP-Rule:MF_00750}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00750, ECO:0000256|RuleBase:RU003969};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00750};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_00750};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00750,
CC       ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|HAMAP-Rule:MF_00750,
CC       ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; LT629777; SDS55291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1T565; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000199524; Chromosome i.
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; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   HAMAP; MF_00750; Choline_dehydrogen; 1.
DR   InterPro; IPR011533; BetA.
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   NCBIfam; TIGR01810; betA; 1.
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; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00750};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00750}; NAD {ECO:0000256|HAMAP-Rule:MF_00750};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00750}; Reference proteome {ECO:0000313|Proteomes:UP000199524}.
FT   DOMAIN          84..107
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          261..275
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          536..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        475
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
FT   BINDING         6..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
SQ   SEQUENCE   567 AA;  62875 MW;  A0BE5ECBC24AEFA8 CRC64;
     MSQEYDYIIV GAGSAGNTIT TRLTEDEGVT VLLLEAGGPD YRFDFRTQMP AALAFPLQGR
     RYNWAYETDP EPHMDGRRME CGRGKGLGGS SLINGMCYIR GNAMDYDGWA KLPGLEDWSY
     LDCLPYFRKA ETRDIGPNDY HGGEGPVRVT TPKAGNNPLF HAMVEAGVQA GYPRTEDLNG
     YQQEGFGPMD RTVTPNGRRS STARGYLDIA KKRSTLTIVT HALTDKVLFE GKRAIGVRYL
     VGSAEERVEA RARKEVIVCS GAIASPQLLQ RSGVGPRKLL ESLDIPVVHD LPGVGENLQD
     HLELYLQYAC TQPVSLYPSL LWWNQPAIGA EWLFNGTGIG ASNQFEAGGF IRTREEFEWP
     NIQYHFLPVA INYNGSNGVK EHGFQAHMGS MRSPSRGRVQ LKSKDPRQHP SILFNYMATE
     QDWQEFRDGI RLTREIMAQP ALDAYRGREI SPGIEVQTDE QLDQFIREHA ETAFHPSCSC
     KMGTDEMAVV DGQGRVHGMQ GLRVVDASIM PIITTGNLNA PTIMIAEKIA DKIRGRQPLP
     RSTAPYHVAG DAPARGKPLR EVSRTAQ
//
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