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ID TRPC_HAEIN Reviewed; 477 AA.
AC P46451;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 06-FEB-2007, entry version 48.
DE Tryptophan biosynthesis protein trpCF [Includes: Indole-3-glycerol
DE phosphate synthase (EC 4.1.1.48) (IGPS); N-(5'-phospho-
DE ribosyl)anthranilate isomerase (EC 5.3.1.24) (PRAI)].
GN Name=trpC; OrderedLocusNames=HI1389.1;
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX MEDLINE=95350630; PubMed=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.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION.
RA Koonin E.V., Rudd K.E.;
RL Submitted (SEP-1995) to Swiss-Prot.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps
CC of tryptophan biosynthetic pathway. The first reaction is
CC catalyzed by the isomerase, coded by the trpF domain; the second
CC reaction is catalyzed by the synthase, coded by the trpC domain.
CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-
CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-
CC phosphate = C(1)-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the trpC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trpF family.
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DR EMBL; L42023; AAC23036.1; -; Genomic_DNA.
DR HSSP; P00909; 1JCM.
DR GenomeReviews; L42023_GR; HI1389.1.
DR KEGG; hin:HI1389.1; -.
DR TIGR; HI1389.1; -.
DR BioCyc; HINF71421:HI1389.1-MONOMER; -.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00134; fused; 1.
DR HAMAP; MF_00135; fused; 1.
DR InterPro; IPR013798; Indole-3-GPS.
DR InterPro; IPR001468; Indole-3-GPS_central.
DR InterPro; IPR001240; PRAI.
DR InterPro; IPR011060; RibP_bd_barrel.
DR Pfam; PF00697; PRAI; 1.
DR ProDom; PD001511; IGPS; 1.
DR PROSITE; PS00614; IGPS; 1.
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Decarboxylase; Isomerase; Lyase;
KW Multifunctional enzyme; Tryptophan biosynthesis.
FT CHAIN 1 477 Tryptophan biosynthesis protein trpCF.
FT /FTId=PRO_0000154279.
FT REGION 13 275 Indole-3-glycerol phosphate synthase.
FT REGION 276 477 N-(5'-phosphoribosyl)anthranilate
FT isomerase.
SQ SEQUENCE 477 AA; 53306 MW; B1435FAEFA24379E CRC64;
MMITQDFTKP IDSATVLQKI VLDKAQWVKA KEKEFPLSQF KQNIQNSDRS FYDALAKGTH
QKPAYILECK KASPSKGLIR AEFNLEEIAN VYKHYASAVS VLTDEKYFQG NFEFLPLVRD
IVSQPVLCKD FMISEYQVYL ARYYQVDAIL LMLSVVNDET YRVLADLAHS LGMGVLTETS
NEEEFERALA LGAKIIGVNN RNLHDLTVDL NRVVELTKKY ADCIPADVRI ISESGIYNHK
QIHQLQKVAH GFLIGSSLMG NQDLNNAVRS VIFGENKVCG LTRAQDVKIV YENGALYGGL
IFAEHSKRSV SLRQAQELVT AAPLRFVGVF QNQEIDFIVK IASQLQLYAV QLHGAETEAF
ITALRQQLPK NTQIWKAISV NTEAQSAVDF TDDLNVDRYI FDSQTANQQG GTGKTFDWSL
IPENLKHKII LAGGISPNNV EQAIAQGCLG LDLNSGVESS AGVKDQEKVR LVFNNIY
//