ID TYRA_HAEIN Reviewed; 377 AA. AC P43902; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 156. DE RecName: Full=T-protein; DE Includes: DE RecName: Full=Chorismate mutase; DE Short=CM; DE EC=5.4.99.5; DE Includes: DE RecName: Full=Prephenate dehydrogenase; DE Short=PDH; DE EC=1.3.1.12; GN Name=tyrA; OrderedLocusNames=HI_1290; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934, CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12; CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4- CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1. CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; CC prephenate from chorismate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC prephenate/arogenate dehydrogenase family. {ECO:0000305}. 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; L42023; AAC22939.1; -; Genomic_DNA. DR PIR; H64114; H64114. DR RefSeq; NP_439442.1; NC_000907.1. DR PDB; 2PV7; X-ray; 2.00 A; A/B=81-377. DR PDBsum; 2PV7; -. DR AlphaFoldDB; P43902; -. DR SMR; P43902; -. DR STRING; 71421.HI_1290; -. DR DNASU; 950220; -. DR EnsemblBacteria; AAC22939; AAC22939; HI_1290. DR KEGG; hin:HI_1290; -. DR PATRIC; fig|71421.8.peg.1342; -. DR eggNOG; COG0287; Bacteria. DR eggNOG; COG1605; Bacteria. DR HOGENOM; CLU_036672_1_1_6; -. DR OrthoDB; 6198144at2; -. DR PhylomeDB; P43902; -. DR BioCyc; HINF71421:G1GJ1-1316-MONOMER; -. DR BRENDA; 1.3.1.12; 2529. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00122; UER00961. DR EvolutionaryTrace; P43902; -. DR Proteomes; UP000000579; 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; IBA:GO_Central. DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IBA:GO_Central. 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; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Cytoplasm; Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Tyrosine biosynthesis. FT CHAIN 1..377 FT /note="T-protein" FT /id="PRO_0000119197" FT DOMAIN 1..92 FT /note="Chorismate mutase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515" FT DOMAIN 101..364 FT /note="Prephenate/arogenate dehydrogenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:2PV7" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 111..121 FT /evidence="ECO:0007829|PDB:2PV7" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:2PV7" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:2PV7" FT STRAND 146..150 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 157..164 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:2PV7" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 182..191 FT /evidence="ECO:0007829|PDB:2PV7" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:2PV7" FT STRAND 214..221 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 227..235 FT /evidence="ECO:0007829|PDB:2PV7" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 245..255 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 257..270 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 277..282 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 286..299 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 303..310 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 317..335 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 339..353 FT /evidence="ECO:0007829|PDB:2PV7" FT HELIX 356..370 FT /evidence="ECO:0007829|PDB:2PV7" SQ SEQUENCE 377 AA; 43022 MW; 319722CFDFDE5791 CRC64; MSFMEALKDL RSEIDSLDRE LIQLFAKRLE LVSQVGKVKH QHGLPIYAPE REIAMLQARR LEAEKAGISA DLIEDVLRRF MRESYANENQ FGFKTINSDI HKIVIVGGYG KLGGLFARYL RASGYPISIL DREDWAVAES ILANADVVIV SVPINLTLET IERLKPYLTE NMLLADLTSV KREPLAKMLE VHTGAVLGLH PMFGADIASM AKQVVVRCDG RFPERYEWLL EQIQIWGAKI YQTNATEHDH NMTYIQALRH FSTFANGLHL SKQPINLANL LALSSPIYRL ELAMIGRLFA QDAELYADII MDKSENLAVI ETLKQTYDEA LTFFENNDRQ GFIDAFHKVR DWFGDYSEQF LKESRQLLQQ ANDLKQG //