TRPA_STAAB
ID TRPA_STAAB Reviewed; 242 AA.
AC Q2YXZ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=SAB1228;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80917.1; -; Genomic_DNA.
DR RefSeq; WP_000163611.1; NC_007622.1.
DR AlphaFoldDB; Q2YXZ6; -.
DR SMR; Q2YXZ6; -.
DR KEGG; sab:SAB1228; -.
DR HOGENOM; CLU_016734_0_0_9; -.
DR OMA; LVMTYWN; -.
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; -; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Tryptophan biosynthesis.
FT CHAIN 1..242
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_1000018291"
FT ACT_SITE 31
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 242 AA; 27144 MW; C04BF808FF0C105C CRC64;
MTKLFIPYIM GDKDLIENAT LLSENGADII EIGVPFSDPV ADGPVIMEAG QQAIKQGITI
DYIFEQLEKH GNQIKCQYVL MTYYNIICHY GEQAFFEKCR DTGVYGLIIP DLPFELSQRL
KQQFSHYGVK IISLVAMTTD DKRIKEIVSH AEGFIYTVTM NATTGQNGAF HPELKRKIES
IKAIANVPVV AGFGIRTPQH VADIKEVADG IVIGSEIVKR FKSNTREEII KYLQSIQQTL
NN