TYRA_HAEIN
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 03-AUG-2022, entry version 151.
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; Proteobacteria; 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}.
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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 OMA; EHDHGMT; -.
DR PhylomeDB; P43902; -.
DR BioCyc; HINF71421:G1GJ1-1316-MON; -.
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; 1.20.59.10; -; 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; IPR003099; Prephen_DH.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF02153; PDH; 1.
DR PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01799; CM_T; 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
