ID G7Z2T5_AZOL4 Unreviewed; 288 AA.
AC G7Z2T5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN Name=pheA {ECO:0000313|EMBL:CBS85697.1};
GN OrderedLocusNames=AZOLI_0294 {ECO:0000313|EMBL:CBS85697.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85697.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00000913};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741}.
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DR EMBL; FQ311868; CBS85697.1; -; Genomic_DNA.
DR RefSeq; WP_014246760.1; NC_016622.1.
DR AlphaFoldDB; G7Z2T5; -.
DR STRING; 862719.AZOLI_0294; -.
DR KEGG; ali:AZOLI_0294; -.
DR HOGENOM; CLU_035008_4_2_5; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000005667; Chromosome.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CBS85697.1};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT DOMAIN 6..181
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 196..273
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 174
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 288 AA; 31381 MW; D052B8D0708C2598 CRC64;
MPTTNIIAFQ GFPGAYSDLA CRNARPTMTT MPCATFEDAF AAVREDRASL AMIPVENSIA
GRVADNHYLL PDGGLHIIGE HFQRVNHQLL APKGATLDSI QTVRSHIQAL SQCQTAIRSL
GLQPINHADT AGAAKEIAAM NDPRHAAIAS SLAAEIYGLD ILKSGIEDAA HNTTRFLILA
REPKLPALGS CKTITTFVFR VRSVPAALYK ALGGFATNGI NMTKLESYMV GGHFTQTQFY
ADVEGHPDER PLRLALEELD FFAREVKILG VYPANPFRYQ ESQRVGED
//
