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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
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MyHits synonymsTRPA_CALBD , B9MKC6 , E072C87F884A9E14
match map segment
ipfam:Trp_syntA ihamap:Trp_synth_alpha ipat:TRP_SYNTHASE_ALPHA  
Legends: 1, ACT_SITE Proton acceptor. {ECO:0000255|HAMAP- Rule:MF_00131}; 2, ipat:TRP_SYNTHASE_ALPHA [T].
ID   TRPA_CALBD              Reviewed;         256 AA.
AC   B9MKC6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   02-NOV-2016, entry version 48.
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};
GN   OrderedLocusNames=Athe_1690;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM
RT   6725.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC       of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.
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: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.
CC       {ECO:0000255|HAMAP-Rule:MF_00131}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
DR   EMBL; CP001393; ACM60784.1; -; Genomic_DNA.
DR   RefSeq; WP_015908114.1; NC_012034.1.
DR   ProteinModelPortal; B9MKC6; -.
DR   STRING; 521460.Athe_1690; -.
DR   PRIDE; B9MKC6; -.
DR   EnsemblBacteria; ACM60784; ACM60784; Athe_1690.
DR   KEGG; ate:Athe_1690; -.
DR   PATRIC; 20900548; VBIAnaThe135187_1775.
DR   eggNOG; ENOG4105F6H; Bacteria.
DR   eggNOG; COG0159; LUCA.
DR   HOGENOM; HOG000223816; -.
DR   KO; K01695; -.
DR   OMA; PVFICPP; -.
DR   OrthoDB; POG091H02IL; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000007723; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
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;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Tryptophan biosynthesis.
FT   CHAIN         1    256       Tryptophan synthase alpha chain.
FT                                /FTId=PRO_1000198697.
FT   ACT_SITE     48     48       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00131}.
FT   ACT_SITE     59     59       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00131}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         8    252       ipfam:Trp_syntA [T]
FT   MYHIT        14    252       ihamap:Trp_synth_alpha [T]
FT   MYHIT        47     60       ipat:TRP_SYNTHASE_ALPHA [T]
SQ   SEQUENCE   256 AA;  29043 MW;  E072C87F884A9E14 CRC64;
     MNFIDERFER LKKEGKKAFI GYVTFGYPTF EETLWFIKLV YSYVDILEIG FPFSDPIADG
     EIIQKASIKA LSEGVKLSHL FESIEKFKKD KPVVLMLYAN TVYKRGIDRF FESCKACGVD
     GVIIPDVSFE ESFEFKEVAE KFGIVYIDLV SISSLERAKM IGRQSRGFLY CVSRKGVTGF
     KGQIDDRIFT FLKELKTVTS TPLAVGFGIK SKEDVQKFKD LADGIVIGSA IITKIDEGKD
     KLEDFLKEIS ESLKDK
//