GenomeNet

Database: UniProt
Entry: A1HS62_9FIRM
LinkDB: A1HS62_9FIRM
Original site: A1HS62_9FIRM 
ID   A1HS62_9FIRM            Unreviewed;       285 AA.
AC   A1HS62;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
DE            Short=PDT {ECO:0000256|RuleBase:RU361254};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
GN   Name=pheA {ECO:0000256|RuleBase:RU361254};
GN   ORFNames=TcarDRAFT_0635 {ECO:0000313|EMBL:EAX47127.1};
OS   Thermosinus carboxydivorans Nor1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Thermosinus.
OX   NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX47127.1, ECO:0000313|Proteomes:UP000005139};
RN   [1] {ECO:0000313|EMBL:EAX47127.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX47127.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAX47127.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX47127.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU361254};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741, ECO:0000256|RuleBase:RU361254}.
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:EAX47127.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAWL01000014; EAX47127.1; -; Genomic_DNA.
DR   RefSeq; WP_007289867.1; NZ_AAWL01000014.1.
DR   AlphaFoldDB; A1HS62; -.
DR   eggNOG; COG0077; Bacteria.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000005139; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13633; PBP2_Sa-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; PF01842; ACT; 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; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU361254};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222,
KW   ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005139}.
FT   DOMAIN          13..190
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          204..281
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            183
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   285 AA;  31311 MW;  25F160C287871FC6 CRC64;
     MALVSTEFMA ERIVGYLGPR GTHSEEVALC LYRGEKGRFI PFASIDAAIR AVETGEVMEC
     LVPVENSLEG SVNITLDTLA HDVNLFITRE MVWPVKHNLL VKAGTKHINV VVSHPQALAQ
     CRHYLARFYP GVELKPVEST AEAAYLVASG AKNHAAIASL RAGEIYGLET VAADIQDNPN
     NYTRFIVLAQ RPADVRSGRR KTSVVCQING ERPGSLCDVL QEFARRNVNL TKIESRPART
     GLGVYIFFLD IDGDIDDDNV HAAVSAVKLK SLWFKNLGSY PVYAV
//
DBGET integrated database retrieval system