TRPE_MYCTO
ID TRPE_MYCTO Reviewed; 516 AA.
AC P9WFX2; I7BEI8; O06127; P67001;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=MT1644;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45913.1; -; Genomic_DNA.
DR PIR; G70556; G70556.
DR RefSeq; WP_003407977.1; NZ_KK341227.1.
DR PDB; 5CWA; X-ray; 2.10 A; A=1-511.
DR PDBsum; 5CWA; -.
DR AlphaFoldDB; P9WFX2; -.
DR SMR; P9WFX2; -.
DR EnsemblBacteria; AAK45913; AAK45913; MT1644.
DR GeneID; 45425577; -.
DR KEGG; mtc:MT1644; -.
DR PATRIC; fig|83331.31.peg.1767; -.
DR HOGENOM; CLU_006493_9_3_11; -.
DR BRENDA; 4.1.3.27; 3445.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00564; trpE_most; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Magnesium; Metal-binding; Tryptophan biosynthesis.
FT CHAIN 1..516
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000428462"
FT BINDING 56
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 283..285
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 324..325
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 439
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 459
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 473..475
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 475
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:5CWA"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:5CWA"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 191..210
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 295..306
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 384..397
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:5CWA"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:5CWA"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:5CWA"
FT HELIX 482..503
FT /evidence="ECO:0007829|PDB:5CWA"
SQ SEQUENCE 516 AA; 55849 MW; EF19CDDE80E802C7 CRC64;
MHADLAATTS REDFRLLAAE HRVVPVTRKV LADSETPLSA YRKLAANRPG TFLLESAENG
RSWSRWSFIG AGAPTALTVR EGQAVWLGAV PKDAPTGGDP LRALQVTLEL LATADRQSEP
GLPPLSGGMV GFFAYDMVRR LERLPERAVD DLCLPDMLLL LATDVAAVDH HEGTITLIAN
AVNWNGTDER VDWAYDDAVA RLDVMTAALG QPLPSTVATF SRPEPRHRAQ RTVEEYGAIV
EYLVDQIAAG EAFQVVPSQR FEMDTDVDPI DVYRILRVTN PSPYMYLLQV PNSDGAVDFS
IVGSSPEALV TVHEGWATTH PIAGTRWRGR TDDEDVLLEK ELLADDKERA EHLMLVDLGR
NDLGRVCTPG TVRVEDYSHI ERYSHVMHLV STVTGKLGEG RTALDAVTAC FPAGTLSGAP
KVRAMELIEE VEKTRRGLYG GVVGYLDFAG NADFAIAIRT ALMRNGTAYV QAGGGVVADS
NGSYEYNEAR NKARAVLNAI AAAETLAAPG ANRSGC
