NSAE_SPHXE
ID NSAE_SPHXE Reviewed; 328 AA.
AC Q9X9Q6;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase;
DE Short=THBPA hydratase-aldolase;
DE EC=4.1.2.45;
DE AltName: Full=2'-hydroxybenzalpyruvate aldolase;
GN Name=nsaE;
OS Sphingobium xenophagum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=121428;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=DSM 6383 / KCTC 2978 / NBRC 107872 / BN6;
RX PubMed=16804169; DOI=10.1099/mic.0.28783-0;
RA Keck A., Conradt D., Mahler A., Stolz A., Mattes R., Klein J.;
RT "Identification and functional analysis of the genes for
RT naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6.";
RL Microbiology 152:1929-1940(2006).
RN [2]
RP PROTEIN SEQUENCE OF 2-27, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=DSM 6383 / KCTC 2978 / NBRC 107872 / BN6;
RX PubMed=8486638; DOI=10.1016/s0021-9258(18)98376-6;
RA Kuhm A.E., Knackmuss H.J., Stolz A.;
RT "Purification and properties of 2'-hydroxybenzalpyruvate aldolase from a
RT bacterium that degrades naphthalenesulfonates.";
RL J. Biol. Chem. 268:9484-9489(1993).
CC -!- FUNCTION: Involved in the naphthalene and naphthalenesulfonate
CC catabolic pathway. Catalyzes the transformation of trans-O-
CC hydroxybenzylidenepyruvate (THBPA) to salicylaldehyde and pyruvate. The
CC reaction is reversible. Can also use 2,4-dihydroxybenzalpyruvate (2,4-
CC DHBP) and 2,6-dihydroxybenzalpyruvate (2,6-DHBP).
CC {ECO:0000269|PubMed:16804169, ECO:0000269|PubMed:8486638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate + H2O = pyruvate +
CC salicylaldehyde; Xref=Rhea:RHEA:27389, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16008, ChEBI:CHEBI:59353; EC=4.1.2.45;
CC Evidence={ECO:0000269|PubMed:8486638};
CC -!- ACTIVITY REGULATION: Inhibited bye p-chloromercuribenzoate and
CC salicylaldehyde. Activated by salicylate. {ECO:0000269|PubMed:16804169,
CC ECO:0000269|PubMed:8486638}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for 2,6-DHBP (at pH 7) {ECO:0000269|PubMed:8486638};
CC KM=15 uM for 2,4-DHBP (at pH 7) {ECO:0000269|PubMed:8486638};
CC KM=17 uM for THBPA (at pH 7) {ECO:0000269|PubMed:8486638};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:8486638};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:8486638}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR EMBL; U65001; AAD45417.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X9Q6; -.
DR SMR; Q9X9Q6; -.
DR KEGG; ag:AAD45417; -.
DR BRENDA; 4.1.2.45; 10830.
DR UniPathway; UPA00082; -.
DR GO; GO:0016832; F:aldehyde-lyase activity; IDA:UniProtKB.
DR GO; GO:0018813; F:trans-o-hydroxybenzylidenepyruvate hydratase-aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; Lyase;
KW Pyruvate.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8486638"
FT CHAIN 2..328
FT /note="Trans-O-hydroxybenzylidenepyruvate hydratase-
FT aldolase"
FT /id="PRO_0000423057"
SQ SEQUENCE 328 AA; 35459 MW; 6A07FAA0E4CEC128 CRC64;
MARTLMKPDD VKGAWAIIPT PAKDDASDWR ATKTVDLDET ARVVNGLIDA GINGILSMGT
LGEAATMTHD EKLDFIKALV DAAAGRVPIF VGTTCLNTRD TIALTRQALD IGADGTMLGV
PMWCAPSVDV AVQFYKDLAE AVPEMNIAIY ANPEAFKFDF PRSFWAQVAE IPQVVTAKYI
GVAHLLPDLA AIRGRIKLLP IDFDYYGAAR MDESIDAFWS SGAVCDPLVT TTLRDLVSQA
RATGDWSAAR AFMGRLGPTA APLFPNGSFK EFSTYNIALE KARMNAGGWM NAGPVRPPYH
LCPEPYLEGA RLSGRMWAEL GKALAAEK