BETB_PSEAE
ID BETB_PSEAE Reviewed; 490 AA.
AC Q9HTJ1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=NAD/NADP-dependent 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=PA5373;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11104673; DOI=10.1042/bj3520675;
RA Velasco-Garcia R., Gonzalez-Segura L., Munoz-Clares R.A.;
RT "Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions
RT catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa.";
RL Biochem. J. 352:675-683(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP AND POTASSIUM
RP IONS, ACTIVE SITE, OXIDATION AT CYS-286, REACTION MECHANISM, COFACTOR, AND
RP SUBUNIT.
RX PubMed=19013472; DOI=10.1016/j.jmb.2008.10.082;
RA Gonzalez-Segura L., Rudino-Pinera E., Munoz-Clares R.A., Horjales E.;
RT "The crystal structure of a ternary complex of betaine aldehyde
RT dehydrogenase from Pseudomonas aeruginosa Provides new insight into the
RT reaction mechanism and shows a novel binding mode of the 2'-phosphate of
RT NADP+ and a novel cation binding site.";
RL J. Mol. Biol. 385:542-557(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-490 IN COMPLEX WITH NADP AND
RP POTASSIUM IONS, AND SUBUNIT.
RA Diaz-Sanchez A.G., Gonzalez-Segura L., Rudino-Pinera E., Lira-Rocha A.,
RA Munoz-Clares R.A.;
RT "A novel cysteine-NADPH covalent adduct in Pseudomonas aeruginosa betaine
RT aldehyde dehydrogenase suggests important roles for the reduced nucleotide
RT in the reaction mechanism.";
RL Submitted (MAY-2010) to the PDB data bank.
RN [5] {ECO:0007744|PDB:2WOX, ECO:0007744|PDB:3ZQA}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-490 OF WILD-TYPE AND MUTANT
RP ALA-286 IN COMPLEX WITH NADP AND POTASSIUM IONS, FUNCTION, COFACTOR,
RP SUBUNIT, AND REACTION MECHANISM.
RX PubMed=21732915; DOI=10.1042/bj20110376;
RA Diaz-Sanchez A.G., Gonzalez-Segura L., Rudino-Pinera E., Lira-Rocha A.,
RA Torres-Larios A., Munoz-Clares R.A.;
RT "Novel NADPH-cysteine covalent adduct found in the active site of an
RT aldehyde dehydrogenase.";
RL Biochem. J. 439:443-452(2011).
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC the corresponding acid. In P.aeruginosa this reaction is a compulsory
CC step in the assimilation of carbon and nitrogen when bacteria are
CC growing in choline or choline precursors. Can use NADP(+) with similar
CC efficiency to NAD(+), a property that can be used by the bacterium to
CC produce the NADPH needed to combat the oxidative stress imposed by the
CC host defenses. {ECO:0000255|HAMAP-Rule:MF_00804,
CC ECO:0000269|PubMed:11104673, ECO:0000269|PubMed:21732915}.
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, ECO:0000269|PubMed:11104673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000305|PubMed:11104673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NADP(+) = glycine betaine + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:30067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:11104673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30068;
CC Evidence={ECO:0000305|PubMed:11104673};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804,
CC ECO:0000269|PubMed:19013472, ECO:0000269|PubMed:21732915};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00804, ECO:0000269|PubMed:19013472,
CC ECO:0000269|PubMed:21732915};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=507 uM for betaine aldehyde (at pH 8.0 and 30 degrees Celsius, in
CC the presence of NADP(+)) {ECO:0000269|PubMed:11104673};
CC KM=434 uM for betaine aldehyde (at pH 8.0 and 30 degrees Celsius, in
CC the presence of NAD(+)) {ECO:0000269|PubMed:11104673};
CC KM=83 uM for NADP(+) (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11104673};
CC KM=385 uM for NAD(+) (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11104673};
CC Note=kcat is 261 sec(-1) for the NADP-dependent oxidation of betaine
CC aldehyde. kcat is 276 sec(-1) for the NAD-dependent oxidation of
CC betaine aldehyde. {ECO:0000269|PubMed:11104673};
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 ECO:0000269|PubMed:19013472, ECO:0000269|PubMed:21732915,
CC ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG08758.1; -; Genomic_DNA.
DR PIR; F82973; F82973.
DR RefSeq; NP_254060.1; NC_002516.2.
DR RefSeq; WP_003114436.1; NZ_QZGE01000031.1.
DR PDB; 2WME; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-490.
DR PDB; 2WOX; X-ray; 2.30 A; A/B/C/D=2-490.
DR PDB; 2XDR; X-ray; 2.30 A; A/B/C/D=2-490.
DR PDB; 3ZQA; X-ray; 2.45 A; A/B/C/D=1-490.
DR PDB; 4CAZ; X-ray; 2.55 A; A/B=1-490.
DR PDB; 4CBB; X-ray; 1.80 A; A/B/C/D/E/F/G/H=2-490.
DR PDB; 6BJP; X-ray; 2.10 A; A/B/C/D=1-490.
DR PDB; 6BPG; X-ray; 3.09 A; A/B/C/D/E/F/G/H=1-490.
DR PDBsum; 2WME; -.
DR PDBsum; 2WOX; -.
DR PDBsum; 2XDR; -.
DR PDBsum; 3ZQA; -.
DR PDBsum; 4CAZ; -.
DR PDBsum; 4CBB; -.
DR PDBsum; 6BJP; -.
DR PDBsum; 6BPG; -.
DR AlphaFoldDB; Q9HTJ1; -.
DR SMR; Q9HTJ1; -.
DR STRING; 287.DR97_2749; -.
DR PaxDb; Q9HTJ1; -.
DR PRIDE; Q9HTJ1; -.
DR DNASU; 881619; -.
DR EnsemblBacteria; AAG08758; AAG08758; PA5373.
DR GeneID; 881619; -.
DR KEGG; pae:PA5373; -.
DR PATRIC; fig|208964.12.peg.5630; -.
DR PseudoCAP; PA5373; -.
DR HOGENOM; CLU_005391_0_2_6; -.
DR InParanoid; Q9HTJ1; -.
DR OMA; AFTASMH; -.
DR PhylomeDB; Q9HTJ1; -.
DR BioCyc; PAER208964:G1FZ6-5500-MON; -.
DR BRENDA; 1.2.1.8; 5087.
DR UniPathway; UPA00529; UER00386.
DR EvolutionaryTrace; Q9HTJ1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NAD; Oxidation; Oxidoreductase; Potassium;
KW Reference proteome.
FT CHAIN 1..490
FT /note="NAD/NADP-dependent betaine aldehyde dehydrogenase"
FT /id="PRO_0000056546"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0000269|PubMed:19013472"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0000269|PubMed:19013472"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:21732915"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0000269|PubMed:19013472"
FT BINDING 26
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT BINDING 27
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT BINDING 150..153
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000269|PubMed:21732915,
FT ECO:0007744|PDB:2WOX"
FT BINDING 176..179
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000269|PubMed:21732915,
FT ECO:0007744|PDB:2WOX"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT BINDING 209
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000269|PubMed:21732915,
FT ECO:0007744|PDB:2WOX"
FT BINDING 230..233
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000269|PubMed:21732915,
FT ECO:0007744|PDB:2WOX"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT BINDING 286
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21732915,
FT ECO:0007744|PDB:2WOX"
FT BINDING 387
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000269|PubMed:21732915,
FT ECO:0007744|PDB:2WOX"
FT BINDING 457
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT SITE 248
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT MOD_RES 286
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0000269|PubMed:19013472"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6BPG"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:4CBB"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:4CBB"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4CBB"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 331..346
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4CBB"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 390..400
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6BPG"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:4CBB"
FT HELIX 466..471
FT /evidence="ECO:0007829|PDB:4CBB"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:4CBB"
SQ SEQUENCE 490 AA; 53332 MW; F48249A085E3A970 CRC64;
MARFEEQKLY IGGRYVEASS GATFETINPA NGEVLAKVQR ASREDVERAV QSAVEGQKVW
AAMTAMQRSR ILRRAVDILR ERNDELAALE TLDTGKPLAE TRSVDIVTGA DVLEYYAGLV
PAIEGEQIPL RETSFVYTRR EPLGVVAGIG AWNYPVQIAL WKSAPALAAG NAMIFKPSEV
TPLTALKLAE IYTEAGVPDG VFNVLTGSGR EVGQWLTEHP LIEKISFTGG TSTGKKVMAS
ASSSSLKEVT MELGGKSPLI IFPDADLDRA ADIAVMANFF SSGQVCTNGT RVFIHRSQQA
RFEAKVLERV QRIRLGDPQD ENTNFGPLVS FPHMESVLGY IESGKAQKAR LLCGGERVTD
GAFGKGAYVA PTVFTDCRDD MTIVREEIFG PVMSILVYDD EDEAIRRAND TEYGLAAGVV
TQDLARAHRA IHRLEAGICW INTWGESPAE MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ
VELGDYASVF
