ID D0I4F7_GRIHO Unreviewed; 375 AA.
AC D0I4F7;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN ORFNames=VHA_000622 {ECO:0000313|EMBL:EEY73374.1};
OS Grimontia hollisae CIP 101886.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY73374.1, ECO:0000313|Proteomes:UP000003604};
RN [1] {ECO:0000313|EMBL:EEY73374.1, ECO:0000313|Proteomes:UP000003604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY73374.1,
RC ECO:0000313|Proteomes:UP000003604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000256|PIRNR:PIRNR001499}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000256|PIRNR:PIRNR001499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001499}.
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:EEY73374.1}.
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DR EMBL; ADAQ01000009; EEY73374.1; -; Genomic_DNA.
DR RefSeq; WP_005501814.1; NZ_ADAQ01000009.1.
DR AlphaFoldDB; D0I4F7; -.
DR GeneID; 58895565; -.
DR eggNOG; COG0287; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR OrthoDB; 6198144at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000003604; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR008244; Chor_mut/prephenate_DH_T.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR011277; CM_T.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR NCBIfam; TIGR01799; CM_T; 1.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001499};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001499};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR001499};
KW Isomerase {ECO:0000256|PIRNR:PIRNR001499};
KW NAD {ECO:0000256|PIRNR:PIRNR001499};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR001499};
KW Reference proteome {ECO:0000313|Proteomes:UP000003604};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR001499}.
FT DOMAIN 1..90
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 99..361
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 375 AA; 42024 MW; 7F3F69AAA9E43F50 CRC64;
MVAELTHLRD QIDDVDKQMV ELLARRLALV AEVGEVKSKH GLPIYAPDRE AAMLASRREE
AASKGVPPDL IEDILRRTMR ESYASENDSG FKCLNPDLRS IVVVGGNGQL GQVFCKLFRL
SGYNVKVLGS QDWHKADEML SDAGMVVITV PINKTDSVIR SLSKLPDDCL LADLTSIKSE
PLQAMLESHK GPVVGLHPMF GPDISSLAKQ VIVYCDGRNP EAYQWLLEQF RIWGASLHRI
SAIEHDQGMT LIQALRHFTS FVYGLHLAEE NANLEQLTAL SSPIYRLELA MVGRLFAQDA
QLYGDIIMSS TQNIDMIKRF HARFGEAINL LDKQDKEGFI TAFNQVENWF GDFAPRFMKE
SQNLLRQAND TAHRG
//
