TRPA_SACS2
ID TRPA_SACS2 Reviewed; 245 AA.
AC P50382;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 132.
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=SSO0889;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RA Tutino M.L., Cubellis M., Sannia G., Marino G.;
RT "The tryptophan operon in Sulfolobus solfataricus.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA90308.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z50014; CAA90308.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006641; AAK41172.1; -; Genomic_DNA.
DR PIR; E90239; E90239.
DR RefSeq; WP_009992303.1; NC_002754.1.
DR PDB; 5N2P; X-ray; 2.06 A; A=4-244.
DR PDB; 6HUL; X-ray; 2.55 A; A=4-244.
DR PDBsum; 5N2P; -.
DR PDBsum; 6HUL; -.
DR AlphaFoldDB; P50382; -.
DR SMR; P50382; -.
DR STRING; 273057.SSO0889; -.
DR EnsemblBacteria; AAK41172; AAK41172; SSO0889.
DR GeneID; 44129820; -.
DR KEGG; sso:SSO0889; -.
DR PATRIC; fig|273057.12.peg.893; -.
DR eggNOG; arCOG01086; Archaea.
DR HOGENOM; CLU_016734_0_2_2; -.
DR InParanoid; P50382; -.
DR OMA; LVMTYWN; -.
DR PhylomeDB; P50382; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001974; 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 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 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..245
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098900"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:5N2P"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:5N2P"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:5N2P"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:5N2P"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:5N2P"
SQ SEQUENCE 245 AA; 27387 MW; AD73236D7CFAC70F CRC64;
MEMGKMLVVY MTLGYPNVQS FKDFIIGAVE NGADILELGI PPKYAKYDGP VIRKSYDKVK
GLDIWPLIED IRKDVGVPII ALTYLEDWVD QLENFLNMIK DVKLDGILFP DLLIDYIDDL
DKIDGIIKNK GLKNVIFTSP SVPDLLIHKV SKISDLFLYY GVRPTTGVPI PVSVKQLINR
VRNLVENKLI VGFGLSSESD LRDALSAGAD GIAIGTVFIE EIERNGVKSA INLVKKFRAI
LDEYK
