ID A0A103DWB6_9BURK Unreviewed; 489 AA.
AC A0A103DWB6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=WS67_22135 {ECO:0000313|EMBL:KVE23906.1};
OS Burkholderia singularis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=1503053 {ECO:0000313|EMBL:KVE23906.1, ECO:0000313|Proteomes:UP000062788};
RN [1] {ECO:0000313|EMBL:KVE23906.1, ECO:0000313|Proteomes:UP000062788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV85 {ECO:0000313|EMBL:KVE23906.1,
RC ECO:0000313|Proteomes:UP000062788};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) 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:KVE23906.1}.
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DR EMBL; LOWA01000056; KVE23906.1; -; Genomic_DNA.
DR RefSeq; WP_059520264.1; NZ_LOWA01000056.1.
DR AlphaFoldDB; A0A103DWB6; -.
DR OrthoDB; 6187633at2; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000062788; 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; 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:UP000062788}.
FT DOMAIN 17..478
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 463
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 26
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 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 229..232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 245
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 386
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 456
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 459
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT SITE 247
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT MOD_RES 285
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
SQ SEQUENCE 489 AA; 52300 MW; CCFD01F8810B85E6 CRC64;
MSVFGLQRLY IAGAYADATS GKTFDTLDPA TGALLATVQQ ASADDIDRAV ASAHEGQREW
AAMSAMQRSR ILRRAVELLR ERNDVLAELE MRDTGKPIAE TRAVDIVTGA DVIEYYAGLA
TAIEGLQVPL RPDSFVYTRR EPLGVCCGIG AWNYPIQIAC WKSAPALAAG NAMIFKPSEV
TPLSALKLAE IYTEAGVPAG VFNVVQGDGT VGALLTAHPG IAKVSFTGGV ETGKKVMSIA
GASSLKEVTM ELGGKSPLIV FDDADLDRAA DIAVTANFFS AGQVCTNGTR VFVQRSVKDT
FVARVLERVA RIRIGKPSDP DTNFGPLASA AQLDKVLGYI ESGKAEGAKL LAGGERLVHD
HFANGQYVAP TVFDGCRDDM KIVREEIFGP VMSILVFDTE DEAIARANAT DYGLAAGVVT
ENLSRAHRAI HRLEAGICWI NTWGESPAEM PVGGYKQSGV GRENGITTLE HYTRIKSVQV
ELGRYQPVF
//
