(data stored in SCRATCH zone)

SWISSPROT: Q13S23_PARXL

ID   Q13S23_PARXL            Unreviewed;       281 AA.
AC   Q13S23;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 91.
DE   RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS00736002};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS00779130};
GN   Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131};
GN   ORFNames=Bxe_B2879 {ECO:0000313|EMBL:ABE33116.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33116.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33116.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33116.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC       of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00131,
CC       ECO:0000256|SAAS:SAAS00779183}.
CC   -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC       phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS00779184}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00131, ECO:0000256|SAAS:SAAS00779140}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS00779159}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00131, ECO:0000256|RuleBase:RU003662,
CC       ECO:0000256|SAAS:SAAS00779181}.
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DR   EMBL; CP000271; ABE33116.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q13S23; -.
DR   STRING; 266265.Bxe_B2879; -.
DR   EnsemblBacteria; ABE33116; ABE33116; Bxe_B2879.
DR   KEGG; bxe:Bxe_B2879; -.
DR   eggNOG; ENOG4105F6H; Bacteria.
DR   eggNOG; COG0159; LUCA.
DR   HOGENOM; HOG000223815; -.
DR   KO; K01695; -.
DR   OMA; DYPPEEC; -.
DR   OrthoDB; POG091H02IL; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP.
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   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;
DR   PRODOM; Q13S23.
DR   SWISS-2DPAGE; Q13S23.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS00779192};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS00779180};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS00779198,
KW   ECO:0000313|EMBL:ABE33116.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS00779179}.
FT   ACT_SITE     60     60       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
FT   ACT_SITE     71     71       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
SQ   SEQUENCE   281 AA;  29679 MW;  7C46F7963470B1F1 CRC64;
     MLRSNSIREY SMSRIKNTFA ALSAQGKKGL IPFMTAGDPD PARTVEFMHA LAAGGADVIE
     LGVPFSDPMA DGPVIQQSSE RALAQGVSLR HVIADVKRFR ETNDTTPVVL MGYANPIERM
     GTEAFARAAK EAGVDGVLVV DYPPEECANF AEQMRSAGID PIFLLAPTST DERIAEVGKI
     ASGYVYYVSL KGVTGAANLD VSSIASKIPA IKSRVPLPVG VGFGIRDAQT ARAVAEVSDA
     VVIGSRIVQL LEQAAPESAA ATLTRFIAEV REALDSVATA R
//

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