ID A0A2S0UMQ5_9RHOB Unreviewed; 484 AA.
AC A0A2S0UMQ5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00804};
DE Short=BADH {ECO:0000256|HAMAP-Rule:MF_00804};
DE EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00804};
GN Name=betB {ECO:0000256|HAMAP-Rule:MF_00804};
GN ORFNames=HYN69_11815 {ECO:0000313|EMBL:AWB49097.1};
OS Gemmobacter aquarius.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=2169400 {ECO:0000313|EMBL:AWB49097.1, ECO:0000313|Proteomes:UP000244496};
RN [1] {ECO:0000313|EMBL:AWB49097.1, ECO:0000313|Proteomes:UP000244496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0069 {ECO:0000313|EMBL:AWB49097.1,
RC ECO:0000313|Proteomes:UP000244496};
RA Yi H., Baek M.-G.;
RT "Genome sequencing of Gemmobacter.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC the corresponding acid. {ECO:0000256|HAMAP-Rule:MF_00804}.
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_00804};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00804};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00804};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000256|HAMAP-Rule:MF_00804}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000256|HAMAP-Rule:MF_00804}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00804, ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00804}.
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DR EMBL; CP028918; AWB49097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0UMQ5; -.
DR KEGG; geh:HYN69_11815; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000244496; Chromosome.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00804; BADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR011264; BADH.
DR NCBIfam; TIGR01804; BADH; 1.
DR PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00804};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00804};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00804};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00804};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00804};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00804};
KW Reference proteome {ECO:0000313|Proteomes:UP000244496}.
FT DOMAIN 16..473
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 458
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 27
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 149..151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 175..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 243
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 381
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 451
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 454
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT MOD_RES 283
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
SQ SEQUENCE 484 AA; 50586 MW; 93B4FC0566747912 CRC64;
MKAQPEASHF VNGAYVEDKA GAPVEVIYPA TGEVIAIVHE ATPAVVEAAL AGAAAAQGAW
AALKPVERAR ILRRAADIIR ARNPELARLE TLDTGKPLQE TLVADWPSGA DALEWFAGLA
PTVTGQTIPL GRDFVYTLRE ALGVCVGLGA WNYPSQIACW KAAPALAMGN AMVFKPSEVT
PLGALKLAEI FVEAGLPAGL FNVVQGRGAV GGSLVTDPRV AKVSLTGSVP TGQKVYAAAA
AGVRHVTMEL GGKSPLVVFD DASVEDAVGA AMLGNFYSAG QVCSNGTRVF VQRGIKERFL
KRLAERTAAI VLGDPLDEAT QMGPLVSAVQ LEKVLGYIEV AKAEGARLVC GGGRAALNTG
YYVQPTVFAD VTDGMTLARE EVFGPVMAVL DFETEDEAIA RANDTEFGLA AGVFTADLAR
AHRVVGQLQA GTTWINAYNL TPVESPFGGS KRSGVGRENG HAAIEHYSQV KSVYVGMGPV
DAPY
//
