TRPA_MYCTU
ID TRPA_MYCTU Reviewed; 270 AA.
AC P9WFY1; L0T7F3; O06130; P66980;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=Rv1613;
GN ORFNames=MTCY01B2.05;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; AL123456; CCP44377.1; -; Genomic_DNA.
DR PIR; C70557; C70557.
DR RefSeq; NP_216129.1; NC_000962.3.
DR RefSeq; WP_003407999.1; NZ_NVQJ01000016.1.
DR PDB; 5OCW; X-ray; 4.00 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-270.
DR PDB; 5TCF; X-ray; 2.46 A; A/C/E/G=1-270.
DR PDB; 5TCG; X-ray; 2.40 A; A/C/E/G=1-270.
DR PDB; 5TCH; X-ray; 2.35 A; A/C/E/G=1-270.
DR PDB; 5TCI; X-ray; 2.45 A; A/C/E/G=1-270.
DR PDB; 5TCJ; X-ray; 2.40 A; A/C/E/G=1-270.
DR PDB; 6DWE; X-ray; 2.69 A; A/C/E/G=1-270.
DR PDB; 6E9P; X-ray; 2.57 A; A/C/E/G=1-270.
DR PDB; 6U6C; X-ray; 2.40 A; A/C/E/G=1-270.
DR PDB; 6UAP; X-ray; 2.75 A; A/C/E/G=1-270.
DR PDB; 6UB9; X-ray; 2.78 A; A/C/E/G=1-270.
DR PDB; 6USA; X-ray; 2.41 A; A/C/E/G=1-270.
DR PDBsum; 5OCW; -.
DR PDBsum; 5TCF; -.
DR PDBsum; 5TCG; -.
DR PDBsum; 5TCH; -.
DR PDBsum; 5TCI; -.
DR PDBsum; 5TCJ; -.
DR PDBsum; 6DWE; -.
DR PDBsum; 6E9P; -.
DR PDBsum; 6U6C; -.
DR PDBsum; 6UAP; -.
DR PDBsum; 6UB9; -.
DR PDBsum; 6USA; -.
DR AlphaFoldDB; P9WFY1; -.
DR SMR; P9WFY1; -.
DR STRING; 83332.Rv1613; -.
DR PaxDb; P9WFY1; -.
DR DNASU; 885291; -.
DR GeneID; 45425581; -.
DR GeneID; 885291; -.
DR KEGG; mtu:Rv1613; -.
DR TubercuList; Rv1613; -.
DR eggNOG; COG0159; Bacteria.
DR OMA; LVMTYWN; -.
DR PhylomeDB; P9WFY1; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..270
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098811"
FT ACT_SITE 57
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:5TCH"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:5TCH"
SQ SEQUENCE 270 AA; 27728 MW; 9B55994F704A9C76 CRC64;
MVAVEQSEAS RLGPVFDSCR ANNRAALIGY LPTGYPDVPA SVAAMTALVE SGCDIIEVGV
PYSDPGMDGP TIARATEAAL RGGVRVRDTL AAVEAISIAG GRAVVMTYWN PVLRYGVDAF
ARDLAAAGGL GLITPDLIPD EAQQWLAASE EHRLDRIFLV APSSTPERLA ATVEASRGFV
YAASTMGVTG ARDAVSQAAP ELVGRVKAVS DIPVGVGLGV RSRAQAAQIA QYADGVIVGS
ALVTALTEGL PRLRALTGEL AAGVRLGMSA
