BETB_RHIEC
ID BETB_RHIEC Reviewed; 487 AA.
AC Q2KB42;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=RHE_CH01137;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC89944.1; -; Genomic_DNA.
DR RefSeq; WP_011424478.1; NC_007761.1.
DR AlphaFoldDB; Q2KB42; -.
DR SMR; Q2KB42; -.
DR STRING; 347834.RHE_CH01137; -.
DR EnsemblBacteria; ABC89944; ABC89944; RHE_CH01137.
DR KEGG; ret:RHE_CH01137; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_5; -.
DR OMA; GMKYVTM; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000001936; 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 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;
KW Reference proteome.
FT CHAIN 1..487
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_1000047052"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 461
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 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 229..232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 244
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 384
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 454
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
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 MOD_RES 284
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
SQ SEQUENCE 487 AA; 51733 MW; E1BDD8086ADCBB1C CRC64;
MKAQPKASHF INGEYVEDTD GTVIESLYPA TGEVIARLHA ATPAIVEKAI AAAKRAQPEW
AAMSPMARGR ILKRAADIMR ERNRELSELE TLDTGKPIQE TIVADPTSGA DAFEFFGGVA
PAGLNGSHIP LGQDFAYTKR VPLGVCVGIG AWNYPQQIAC WKGAPALISG NAMVFKPSEN
TPLGALKIAE ILHEAGLPKG LFNVIQGDRD TGPLLVNHPD VAKVSLTGSV PTGRRVAAAA
AGSLKHVTME LGGKSPLIVF DDADLDSAVG GAMLGNFYST GQVCSNGTRV FVQKAVKAEF
LKRLKARTEA MLIGDPLDEA TQIGPMVSWA QREKVIAYIE KGKAEGATLV AGGGIPNNVS
GEGYYVQPTV FADVTDDMTI AREEIFGPVM SVLDFDDEDE VITRANASEF GLSGGVFTAD
LSRAHRVVDR LEAGTLWINT YNLCPVEIPF GGSKQSGFGR ENSLAALEHY SELKTVYVGM
GPVAAPY
