ID A0A0F5V9H4_9GAMM Unreviewed; 486 AA.
AC A0A0F5V9H4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=KY46_16795 {ECO:0000313|EMBL:KKC98778.1};
OS Photobacterium halotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=265726 {ECO:0000313|EMBL:KKC98778.1, ECO:0000313|Proteomes:UP000033633};
RN [1] {ECO:0000313|EMBL:KKC98778.1, ECO:0000313|Proteomes:UP000033633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MELD1 {ECO:0000313|EMBL:KKC98778.1,
RC ECO:0000313|Proteomes:UP000033633};
RA Mathew D.C., Huang C.-C.;
RT "Mercury Reductase activity and rhizosphere competence traits in the genome
RT of root associated Photobacterium halotolerans MELD1.";
RL Submitted (DEC-2014) 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}.
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:KKC98778.1}.
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DR EMBL; JWYV01000016; KKC98778.1; -; Genomic_DNA.
DR RefSeq; WP_046221774.1; NZ_JWYV01000016.1.
DR AlphaFoldDB; A0A0F5V9H4; -.
DR STRING; 265726.KY46_16795; -.
DR PATRIC; fig|265726.11.peg.1627; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000033633; Unassembled WGS sequence.
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 CDD; cd07090; ALDH_F9_TMBADH; 1.
DR HAMAP; MF_00804; BADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
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; 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:UP000033633}.
FT DOMAIN 16..474
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 459
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 23
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 90
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 147..149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 173..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 241
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 452
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 455
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT SITE 243
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT MOD_RES 281
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
SQ SEQUENCE 486 AA; 52323 MW; 0E00FDC745464697 CRC64;
MTMTSLYIHG QATQATSGEQ FETRNPATGE VIARVGQASE ADMARAIASA KEGFAIWSAM
SGAERGRILM KAVALLRERN DELAALEVQD TGKPLQEALE VDIVTGADVI EYYAGLAASL
SGQQQDLGHG QFFYTRREPL GICAGIGAWN YPIQIAMWKS APALAAGNAM IFKPSEETPL
TALKLAEIYT EAGVPDGVFN VVQGDYRVGQ MLSRHPEIAK VSFTGECGTG KKVMADAAGT
LKDVTMELGG KSPLIVFDDA QLDNAVSAAM MANFYTQGEV CTHGTRVFVH DAVYDEFLKR
LAARTALLKV GDPSDINTQI GALISTEHLE KVLGFIEAGK QSGARLLAGG HRVTENGLDK
GNFVAPTIFA DCTDDMPQVK EEIFGPVMSV LRFHEEDEVI RRANDTDYGL AAGIFTQNLS
RAHRLIAQIE AGICWINTWG GSPAEMPVGG YKHSGVGREN GLETLNHYTQ TKSVLIELGD
LECPYL
//
