ID L0MEP1_9GAMM Unreviewed; 373 AA.
AC L0MEP1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN ORFNames=D781_0840 {ECO:0000313|EMBL:AGB81181.1};
OS Serratia sp. FGI94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB81181.1, ECO:0000313|Proteomes:UP000011001};
RN [1] {ECO:0000313|EMBL:AGB81181.1, ECO:0000313|Proteomes:UP000011001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI94 {ECO:0000313|EMBL:AGB81181.1,
RC ECO:0000313|Proteomes:UP000011001};
RX PubMed=23516234;
RA Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT Leaf-Cutter Ant Fungus Gardens.";
RL Genome Announc. 1:E0023912-E0023912(2013).
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}.
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DR EMBL; CP003942; AGB81181.1; -; Genomic_DNA.
DR RefSeq; WP_015671033.1; NC_020064.1.
DR AlphaFoldDB; L0MEP1; -.
DR GeneID; 61764356; -.
DR KEGG; smaf:D781_0840; -.
DR PATRIC; fig|1249634.3.peg.786; -.
DR eggNOG; COG0287; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR HOGENOM; CLU_036672_1_1_6; -.
DR OrthoDB; 6198144at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000011001; Chromosome.
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 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 373 AA; 42081 MW; C3F6093B09879B25 CRC64;
MVAELTALRD QIDEVDKALL DLLAKRLHLV AEVGEVKSRY GLPVYVPERE AAMLASRRQE
AETLGVPPDL IEDILRRVMR ESYTSENDKG FKTLCPQLRP IVIIGGNGQM GRLFNRLLTL
SGYQVKVLDQ QDWPQAESLL SDAGMVIVSV PIHVTEQVIG RLPKLPDDCI LVDLASVKNP
PLQAMLSAHS GPVLGLHPMF GPDVGSVAKQ VVVYCDGRQP EAYQWLLEQL QVWGARLHRI
SAVEHDQNMA FIQALRHFAT FAYGLHLAEE NVQLEQLLAL SSPIYRLELA MVGRLFAQDP
QLYADIIMSS GDNLQLIKRY YARFGEAIQL LEQGDKQAFI DSFRKVEHWF GDYAQRFLVE
SRSLLRQAND SRR
//
