TRPA_STRPN
ID TRPA_STRPN Reviewed; 258 AA.
AC Q97P33;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SP_1811;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; AE005672; AAK75884.1; -; Genomic_DNA.
DR PIR; C95211; C95211.
DR RefSeq; WP_001126999.1; NZ_AKVY01000001.1.
DR PDB; 5KIN; X-ray; 2.45 A; A/C=1-258.
DR PDB; 6QKY; X-ray; 2.54 A; A/B/C/D/E/F/G/H/I/J=1-258.
DR PDBsum; 5KIN; -.
DR PDBsum; 6QKY; -.
DR AlphaFoldDB; Q97P33; -.
DR SMR; Q97P33; -.
DR STRING; 170187.SP_1811; -.
DR EnsemblBacteria; AAK75884; AAK75884; SP_1811.
DR KEGG; spn:SP_1811; -.
DR eggNOG; COG0159; Bacteria.
DR OMA; LVMTYWN; -.
DR PhylomeDB; Q97P33; -.
DR BioCyc; SPNE170187:G1FZB-1843-MON; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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; Tryptophan biosynthesis.
FT CHAIN 1..258
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098854"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:5KIN"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:5KIN"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6QKY"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:5KIN"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:5KIN"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:5KIN"
SQ SEQUENCE 258 AA; 27739 MW; C8044D31CC6E3D8B CRC64;
MPKTLTEKLN AIKAAGKGIF VPYIMAGDHE KGLDGLAETI HFLEDLGVSA IEVGIPFSDP
VADGPVIEEA GLRSLAHGTS TQALVETLKT IETEIPLVIM TYFNPLFQYG VENFVKDLAD
TAVKGLIIPD LPHEHANFVE PFLANTDIAL IPLVSLTTGI ERQKELIEGA EGFIYAVAIN
GVTGKSGNYR ADLDKHLAQL HQVADIPVLT GFGVSSQADL ERFNAVSDGV IVGSKIVKAL
HQGEPIQDFI RQAVAYQK
