TRPA_VIBCH
ID TRPA_VIBCH Reviewed; 268 AA.
AC Q9KST7;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=VC_1169;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE003852; AAF94328.1; -; Genomic_DNA.
DR PIR; D82232; D82232.
DR RefSeq; NP_230814.1; NC_002505.1.
DR RefSeq; WP_001083161.1; NZ_LT906614.1.
DR PDB; 3NAV; X-ray; 2.10 A; A/B=1-268.
DR PDBsum; 3NAV; -.
DR AlphaFoldDB; Q9KST7; -.
DR SMR; Q9KST7; -.
DR STRING; 243277.VC_1169; -.
DR DNASU; 2614602; -.
DR EnsemblBacteria; AAF94328; AAF94328; VC_1169.
DR KEGG; vch:VC_1169; -.
DR PATRIC; fig|243277.26.peg.1118; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_4_6; -.
DR OMA; LVMTYWN; -.
DR BioCyc; VCHO:VC1169-MON; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000584; Chromosome 1.
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 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..268
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098868"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:3NAV"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:3NAV"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3NAV"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:3NAV"
SQ SEQUENCE 268 AA; 28494 MW; A04BEA6FAEECB028 CRC64;
MNRYQALFQR LSAAQQGAFV PFVTIGDPNP EQSLAIMQTL IDAGADALEL GMPFSDPLAD
GPTIQGANLR ALAAKTTPDI CFELIAQIRA RNPETPIGLL MYANLVYARG IDDFYQRCQK
AGVDSVLIAD VPTNESQPFV AAAEKFGIQP IFIAPPTASD ETLRAVAQLG KGYTYLLSRA
GVTGAETKAN MPVHALLERL QQFDAPPALL GFGISEPAQV KQAIEAGAAG AISGSAVVKI
IETHLDNPAK QLTELANFTQ AMKKATKI
