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Database: UniProt
Entry: W9T380_9PSED
LinkDB: W9T380_9PSED
Original site: W9T380_9PSED 
ID   W9T380_9PSED            Unreviewed;       264 AA.
AC   W9T380;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=2-keto-4-pentenoate hydratase {ECO:0000256|HAMAP-Rule:MF_01655};
DE            EC=4.2.1.80 {ECO:0000256|HAMAP-Rule:MF_01655};
DE   AltName: Full=2-hydroxypentadienoic acid hydratase {ECO:0000256|HAMAP-Rule:MF_01655};
GN   Name=mhpD_1 {ECO:0000313|EMBL:EXF45017.1};
GN   Synonyms=mhpD {ECO:0000256|HAMAP-Rule:MF_01655};
GN   ORFNames=BAY1663_02525 {ECO:0000313|EMBL:EXF45017.1};
OS   Pseudomonas sp. BAY1663.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF45017.1, ECO:0000313|Proteomes:UP000019475};
RN   [1] {ECO:0000313|EMBL:EXF45017.1, ECO:0000313|Proteomes:UP000019475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAY1663 {ECO:0000313|EMBL:EXF45017.1,
RC   ECO:0000313|Proteomes:UP000019475};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of Pseudomonas sp. BAY1663.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 2-hydroxypentadienoic acid
CC       (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid.
CC       {ECO:0000256|HAMAP-Rule:MF_01655}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-
CC         dienoate + H2O; Xref=Rhea:RHEA:22580, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:67152, ChEBI:CHEBI:73143; EC=4.2.1.80;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01655};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01655};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_01655}.
CC   -!- SIMILARITY: Belongs to the hydratase/decarboxylase family. MhpD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01655}.
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:EXF45017.1}.
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DR   EMBL; AZSV01000032; EXF45017.1; -; Genomic_DNA.
DR   RefSeq; WP_037040649.1; NZ_AZSV01000032.1.
DR   AlphaFoldDB; W9T380; -.
DR   STRING; 1439940.BAY1663_02525; -.
DR   PATRIC; fig|1439940.3.peg.2489; -.
DR   eggNOG; COG3971; Bacteria.
DR   OrthoDB; 9792137at2; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000019475; Unassembled WGS sequence.
DR   GO; GO:0008684; F:2-oxopent-4-enoate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   HAMAP; MF_01655; MhpD; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR023793; Keto_pentenoate-hydratase.
DR   PANTHER; PTHR30143:SF0; 2-KETO-4-PENTENOATE HYDRATASE; 1.
DR   PANTHER; PTHR30143; ACID HYDRATASE; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW   ECO:0000256|HAMAP-Rule:MF_01655};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01655, ECO:0000313|EMBL:EXF45017.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019475}.
FT   DOMAIN          71..261
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   264 AA;  27777 MW;  27B0821D971E6C1E CRC64;
     MSVTQDILEQ LAAALRAAEC SGEAITPLRE RIGEDAGEAA YAIQRLNVAH AEAAGRRVVG
     RKIGLTNPKV QAQLGVDQPD FGTLFADMCY GDNETVPFGR VMQPKIEAEI ALILHRDLPR
     ADTTFAELLE ATGWVLPSLE IVGSRVQGWN IRFVDTVADN ASSGCFVLGG PALPVAGVDL
     RKASMSMTRN GELVCTGSGA ECLGHPLNAA VWLARTMARL GQPLRAGDIV LTGALGPMVG
     VNPGDRFEAV IEGVGQVAAT FSAE
//
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