TRPE_MYCS2
ID TRPE_MYCS2 Reviewed; 524 AA.
AC A0QX93; I7GAR3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=MSMEG_3217, MSMEI_3135;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP PUPYLATION AT LYS-355, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
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; CP000480; ABK74885.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39599.1; -; Genomic_DNA.
DR RefSeq; WP_003894606.1; NZ_SIJM01000015.1.
DR RefSeq; YP_887531.1; NC_008596.1.
DR PDB; 7BVD; X-ray; 1.70 A; A/B=1-524.
DR PDBsum; 7BVD; -.
DR AlphaFoldDB; A0QX93; -.
DR SMR; A0QX93; -.
DR STRING; 246196.MSMEI_3135; -.
DR EnsemblBacteria; ABK74885; ABK74885; MSMEG_3217.
DR EnsemblBacteria; AFP39599; AFP39599; MSMEI_3135.
DR GeneID; 66734617; -.
DR KEGG; msg:MSMEI_3135; -.
DR KEGG; msm:MSMEG_3217; -.
DR PATRIC; fig|246196.19.peg.3179; -.
DR eggNOG; COG0147; Bacteria.
DR OMA; GCVGYLD; -.
DR OrthoDB; 1786019at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 Isopeptide bond; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Tryptophan biosynthesis; Ubl conjugation.
FT CHAIN 1..524
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000396112"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 298..300
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 339..340
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 454
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 474
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 488..490
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 490
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CROSSLNK 355
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:7BVD"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7BVD"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 206..224
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 364..379
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 388..397
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 402..412
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:7BVD"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:7BVD"
FT STRAND 482..488
FT /evidence="ECO:0007829|PDB:7BVD"
FT HELIX 497..518
FT /evidence="ECO:0007829|PDB:7BVD"
SQ SEQUENCE 524 AA; 56311 MW; 20535CB359AF510F CRC64;
MQTTANHSSR STQTGTRAHG AALAETTSRE DFRALATEHR VVPVIRKVLA DSETPLSAYR
KLAANRPGTF LLESAENGRS WSRWSFIGAG APSALTVRDN AAAWLGTAPE GAPSGGDPLD
ALRATLDLLK TEAMAGLPPL SSGLVGFFAY DMVRRLERLP ELAVDDLGLP DMLLLLATDI
AAVDHHEGTI TLIANAVNWN GTDERVDWAY DDAVARLDVM TKALGQPLTS AVATFSRPAP
DHRAQRTMEE YTEIVDKLVG DIEAGEAFQV VPSQRFEMDT AADPLDVYRI LRVTNPSPYM
YLLNIPDADG GLDFSIVGSS PEALVTVKDG RATTHPIAGT RWRGATEEED VLLEKELLAD
EKERAEHLML VDLGRNDLGR VCRPGTVRVD DYSHIERYSH VMHLVSTVTG ELAEDKTALD
AVTACFPAGT LSGAPKVRAM ELIEEVEKTR RGLYGGVVGY LDFAGNADFA IAIRTALMRN
GTAYVQAGGG VVADSNGPYE YTEAANKARA VLNAIAAAAT LAEP
