MDLD_PSEPU
ID MDLD_PSEPU Reviewed; 436 AA.
AC Q84DC3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=NAD(P)-dependent benzaldehyde dehydrogenase;
DE EC=1.2.1.28;
DE EC=1.2.1.7;
GN Name=mdlD;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90;
RX PubMed=2271624; DOI=10.1021/bi00494a015;
RA Tsou A.Y., Ransom S.C., Gerlt J.A., Buechter D.D., Babbitt P.C.,
RA Kenyon G.L.;
RT "Mandelate pathway of Pseudomonas putida: sequence relationships involving
RT mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate
RT decarboxylase and expression of benzoylformate decarboxylase in Escherichia
RT coli.";
RL Biochemistry 29:9856-9862(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90;
RX PubMed=12670968; DOI=10.1128/jb.185.8.2451-2456.2003;
RA McLeish M.J., Kneen M.M., Gopalakrishna K.N., Koo C.W., Babbitt P.C.,
RA Gerlt J.A., Kenyon G.L.;
RT "Identification and characterization of a mandelamide hydrolase and an
RT NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC
RT 12633.";
RL J. Bacteriol. 185:2451-2456(2003).
CC -!- FUNCTION: NAD or NADP-dependent benzaldehyde dehydrogenase that
CC catalyzes the conversion of benzaldehyde into benzoate in the (R)-
CC mandelate degradation pathway. {ECO:0000269|PubMed:12670968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NADP(+) = benzoate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:21660, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.7;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63.4 uM for benzaldehyde (with NAD) {ECO:0000269|PubMed:12670968};
CC KM=39.9 uM for benzaldehyde (with NADP)
CC {ECO:0000269|PubMed:12670968};
CC Note=kcat is 8240 min (-1) with benzaldehyde and NAD as substrate.
CC kcat is 2550 min (-1) with benzaldehyde and NADP as substrate.;
CC -!- PATHWAY: Aromatic compound metabolism; (R)-mandelate degradation;
CC benzoate from (R)-mandelate: step 4/4.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AY143338; AAO23020.1; -; Genomic_DNA.
DR RefSeq; WP_016501743.1; NZ_UGUX01000003.1.
DR PDB; 5UCD; X-ray; 2.28 A; A/B=1-436.
DR PDBsum; 5UCD; -.
DR AlphaFoldDB; Q84DC3; -.
DR SMR; Q84DC3; -.
DR GeneID; 45526283; -.
DR BioCyc; MetaCyc:MON-2425; -.
DR UniPathway; UPA00873; UER00855.
DR EvolutionaryTrace; Q84DC3; -.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; TAS:UniProtKB.
DR GO; GO:0018477; F:benzaldehyde dehydrogenase (NADP+) activity; TAS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0019596; P:mandelate catabolic process; TAS:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..436
FT /note="NAD(P)-dependent benzaldehyde dehydrogenase"
FT /id="PRO_0000429131"
FT ACT_SITE 215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 117..119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 143..147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 175..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 193..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 215..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 337..339
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:5UCD"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:5UCD"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:5UCD"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:5UCD"
FT HELIX 420..425
FT /evidence="ECO:0007829|PDB:5UCD"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:5UCD"
SQ SEQUENCE 436 AA; 47435 MW; 9E199DB0830B7DE2 CRC64;
MNYLSPAKID SLFSAQKAYF ATRATADVGF RKQSLERLKE AVINNKEALY SALAEDLGKP
KDVVDLAEIG AVLHEIDFAL AHLDEWVAPV SVPSPDIIAP SECYVVQEPY GVTYIIGPFN
YPVNLTLTPL IGAIIGGNTC IIKPSETTPE TSAVIEKIIA EAFAPEYVAV IQGGRDENSH
LLSLPFDFIF FTGSPNVGKV VMQAAAKHLT PVVLELGGKC PLIVLPDADL DQTVNQLMFG
KFINSGQTCI APDYLYVHYS VKDALLERLV ERVKTELPEI NSTGKLVTER QVQRLVSLLE
ATQGQVLVGS QADVSKRALS ATVVDGVEWN DPLMSEELFG PILPVLEFDS VRTAIDQVNK
HHPKPLAVYV FGKDMDVAKG IINQIQSGDA QVNGVMLHAF SPYLPFGGIG ASGMGEYHGH
FSYLTFTHKK SVRIVP
