ID I8I4W8_9GAMM Unreviewed; 313 AA.
AC I8I4W8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase {ECO:0000256|ARBA:ARBA00035695};
DE EC=4.1.2.45 {ECO:0000256|ARBA:ARBA00035679};
DE AltName: Full=2'-hydroxybenzalpyruvate aldolase {ECO:0000256|ARBA:ARBA00035718};
GN ORFNames=WQQ_14730 {ECO:0000313|EMBL:EIT71336.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT71336.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT71336.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT71336.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(2012).
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:0000256|ARBA:ARBA00035599};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000256|ARBA:ARBA00035632}.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIT71336.1}.
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DR EMBL; AKGD01000001; EIT71336.1; -; Genomic_DNA.
DR AlphaFoldDB; I8I4W8; -.
DR STRING; 1172194.WQQ_14730; -.
DR PATRIC; fig|1172194.4.peg.1420; -.
DR Proteomes; UP000003704; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd00952; CHBPH_aldolase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR048038; HBPHA/CBPHA.
DR PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000003704}.
SQ SEQUENCE 313 AA; 34227 MW; 41FD1B7912E27311 CRC64;
MPTPATPDAG DWRVQNTVDL DETARAAEKL IAAGVDAIVT LGSLGECATL TWEEKRAYLG
TLVETVRGRV PLFGGTSSLG TRETIRQTRE ARDIGIDGVM LGPPMWCAPD VPTAVQFYRD
VAEACPDTAI CIYANPEAFK FDFPRPFWAQ VAEIPQVITA KYLGIGALMA DLNLTKGRIR
FLPIDADYYA AARIAPEACT AFWTSGAVCG PAPVLRLRDE VERAKKCGDW AQAQALTGAI
GRTYQTLFPQ GSFKEFSLYN IGLEKARMDA AGWMRAGPAR PPYTLVPEAY LEGARESGRR
WAQLHREYDS RGG
//
