BETB_ECODH
ID BETB_ECODH Reviewed; 490 AA.
AC B1XET7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00804};
DE Short=BADH {ECO:0000255|HAMAP-Rule:MF_00804};
DE EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN Name=betB {ECO:0000255|HAMAP-Rule:MF_00804};
GN OrderedLocusNames=ECDH10B_0299;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00804}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
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DR EMBL; CP000948; ACB01477.1; -; Genomic_DNA.
DR RefSeq; WP_000089110.1; NC_010473.1.
DR AlphaFoldDB; B1XET7; -.
DR SMR; B1XET7; -.
DR PRIDE; B1XET7; -.
DR KEGG; ecd:ECDH10B_0299; -.
DR HOGENOM; CLU_005391_0_0_6; -.
DR OMA; GMKYVTM; -.
DR BioCyc; ECOL316385:ECDH10B_RS01525-MON; -.
DR UniPathway; UPA00529; UER00386.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01804; BADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; NADP; Oxidation; Oxidoreductase; Potassium.
FT CHAIN 1..490
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_1000133950"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 26
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 27
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 230..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 387
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 457
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT SITE 248
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT MOD_RES 286
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
SQ SEQUENCE 490 AA; 52911 MW; 747F822DA1233808 CRC64;
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW
ASMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE TSTVDIVTGA DVLEYYAGLI
PALEGSQIPL RETSFVYTRR EPLGVVAGIG AWNYPIQIAL WKSAPALAAG NAMIFKPSEV
TPLTALKLAE IYSEAGLPDG VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN
SAASSLKEVT MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCKA
AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR VLCGGDVLKG
DGFDNGAWVA PTVFTDCSDD MTIVREEIFG PVMSILTYES EDEVIRRAND TDYGLAAGIV
TADLNRAHRV IHQLEAGICW INTWGESPAE MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ
VEMAKFQSIF
