ID A3F3G4_BACIU Unreviewed; 267 AA.
AC A3F3G4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131,
GN ECO:0000313|EMBL:ABN13207.1};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:ABN13207.1};
RN [1] {ECO:0000313|EMBL:ABN13207.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=23 {ECO:0000313|EMBL:ABN13207.1}, MU8U5U1
RC {ECO:0000313|EMBL:ABN13340.1}, PS832 {ECO:0000313|EMBL:ABN13359.1},
RC PY79 {ECO:0000313|EMBL:ABN13378.1}, W168
RC {ECO:0000313|EMBL:ABN13397.1}, and W23SR
RC {ECO:0000313|EMBL:ABN13245.1};
RX PubMed=18723616; DOI=10.1128/JB.00722-08;
RA Zeigler D.R., Pragai Z., Rodriguez S., Chevreux B., Muffler A., Albert T.,
RA Bai R., Wyss M., Perkins J.B.;
RT "The origins of 168, W23, and other Bacillus subtilis legacy strains.";
RL J. Bacteriol. 190:6983-6995(2008).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000256|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:0000256|ARBA:ARBA00000003, ECO:0000256|HAMAP-
CC Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|HAMAP-Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00131, ECO:0000256|RuleBase:RU003662}.
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DR EMBL; EF191537; ABN13207.1; -; Genomic_DNA.
DR EMBL; EF191539; ABN13245.1; -; Genomic_DNA.
DR EMBL; EF191544; ABN13340.1; -; Genomic_DNA.
DR EMBL; EF191545; ABN13359.1; -; Genomic_DNA.
DR EMBL; EF191546; ABN13378.1; -; Genomic_DNA.
DR EMBL; EF191547; ABN13397.1; -; Genomic_DNA.
DR RefSeq; WP_003225540.1; NZ_QSNC01000001.1.
DR GeneID; 64304043; -.
DR PATRIC; fig|1423.172.peg.3985; -.
DR UniPathway; UPA00035; UER00044.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00262; trpA; 1.
DR PANTHER; PTHR43406:SF1; TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00131};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00131};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00131};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 267 AA; 29378 MW; ECFE99C954E3252F CRC64;
MFKLDLQASE KLFIPFITAG DPSPEVSVKL AKSLQKAGAT ALELGVAYSD PLADGPVIQR
ASKRALDHGM NIVKAIELGG EMKKNGVNIP IILFTYYNPV LQLNKEYFFA LLRKNHIDGL
LVPDLPLEES ASLQADCKNH EVTYISLVAP TSESRLKTII EQAEGFVYCV SSLGVTGVRN
EFNSSVYPFI RTVKDLSTVP VAVGFGISNR EQVMKMNEIC DGVVVGSALV RKIEELKDRL
ISTETRDQAL QEFEDYARAF GGLYSLK
//
