ID A0A0F4Q2P9_9GAMM Unreviewed; 379 AA.
AC A0A0F4Q2P9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN Name=tyrA {ECO:0000313|EMBL:KJZ01100.1};
GN ORFNames=TW72_04430 {ECO:0000313|EMBL:KJZ01100.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJZ01100.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJZ01100.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJZ01100.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ01100.1}.
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DR EMBL; JXXZ01000004; KJZ01100.1; -; Genomic_DNA.
DR RefSeq; WP_045978187.1; NZ_PNCF01000001.1.
DR AlphaFoldDB; A0A0F4Q2P9; -.
DR GeneID; 58227733; -.
DR PATRIC; fig|151081.8.peg.233; -.
DR eggNOG; COG0287; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR OrthoDB; 6198144at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000033664; 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, ECO:0000313|EMBL:KJZ01100.1};
KW NAD {ECO:0000256|PIRNR:PIRNR001499};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR001499};
KW Reference proteome {ECO:0000313|Proteomes:UP000033664};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR001499}.
FT DOMAIN 1..92
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 100..365
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 379 AA; 42007 MW; 9222FAF9E48B8F48 CRC64;
MTSEQQLAQL RNQIDACDTE LVRLLAKRNQ ITEQVGKIKQ QSGAPLHAPE REAALIAARR
KEAEEAAVNP DLVEDILRRM MREAYQNQQS ELACVCKSLN PVAIVGGRGA MGQLFAKQLT
RSGVAVRIID RQEQQSGEAA KLLKGAKCVL ISVPINAVEE VVANLPALDE DALLVDITSV
KEKPLAALTN KHSGPVLGLH PMFGPDISHW VKQTVVVCKD VESEAGEALL AQLKVWGCQL
VTMSARKHDE AMQIIQVMRH LTTFVYGQFL AKQEHSLAEI RDCSSPIYQL ELMMVGRLFA
QSPELYSDIM LAQFERVEPL LEAYKNTYEH TLSMLRDKDK EALMTAFSDA KVFFSDASDQ
FLSQSRALLN KANDAKVLG
//
