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Database: UniProt
Entry: Q9HTJ1
LinkDB: Q9HTJ1
Original site: Q9HTJ1 
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   27-MAR-2024, entry version 140.
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; Pseudomonadota; 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}.
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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; 208964.PA5373; -.
DR   PaxDb; 208964-PA5373; -.
DR   DNASU; 881619; -.
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   OrthoDB; 9812625at2; -.
DR   PhylomeDB; Q9HTJ1; -.
DR   BioCyc; PAER208964:G1FZ6-5500-MONOMER; -.
DR   BRENDA; 1.2.1.8; 5087.
DR   UniPathway; UPA00529; UER00386.
DR   EvolutionaryTrace; Q9HTJ1; -.
DR   Proteomes; UP000002438; Chromosome.
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   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   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
//
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