TRPA_CHLTR
ID TRPA_CHLTR Reviewed; 253 AA.
AC O84173;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Tryptophan synthase alpha chain;
DE EC=4.2.1.20;
GN Name=trpA; OrderedLocusNames=CT_171;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000250}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000305}.
CC -!- CAUTION: This TrpA is highly divergent compared to other bacterial
CC TrpA. As C.trachomatis seems to have lost part of the trp biosynthetic
CC operon, it is possible that this protein is not active. {ECO:0000305}.
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DR EMBL; AE001273; AAC67762.1; -; Genomic_DNA.
DR PIR; B71547; B71547.
DR RefSeq; NP_219674.1; NC_000117.1.
DR RefSeq; WP_010725110.1; NC_000117.1.
DR PDB; 6V82; X-ray; 2.42 A; A=1-253.
DR PDBsum; 6V82; -.
DR AlphaFoldDB; O84173; -.
DR SMR; O84173; -.
DR STRING; 813.O172_00915; -.
DR EnsemblBacteria; AAC67762; AAC67762; CT_171.
DR GeneID; 884962; -.
DR KEGG; ctr:CT_171; -.
DR PATRIC; fig|272561.5.peg.184; -.
DR HOGENOM; CLU_016734_0_0_0; -.
DR InParanoid; O84173; -.
DR OMA; LVMTYWN; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 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..253
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098768"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10120"
FT ACT_SITE 55
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10120"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:6V82"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:6V82"
SQ SEQUENCE 253 AA; 28056 MW; D1A704445C630AEA CRC64;
MSKLTQVFKQ TKLCIGYLTA GDGGTSYTIE AAKALIQGGV DILELGFPFS DPVADNPEIQ
VSHDRALAEN LTSETLLEIV EGIRAFNQEV PLILYSYYNP LLQRDLDYLR RLKDAGINGV
CVIDLPAPLS HGEKSPFFED LLAVGLDPIL LISAGTTPER MSLIQEYARG FLYYIPCQAT
RDSEVGIKEE FRKVREHFDL PIVDRRDICD KKEAAHVLNY SDGFIVKTAF VHQTTMDSSV
ETLTALAQTV IPG
