(data stored in SCRATCH zone)

SWISSPROT: C1AT53_RHOOB

ID   C1AT53_RHOOB            Unreviewed;       267 AA.
AC   C1AT53;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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   ECO:0000313|EMBL:BAH48985.1};
GN   OrderedLocusNames=ROP_07380 {ECO:0000313|EMBL:BAH48985.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48985.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48985.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48985.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-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: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; AP011115; BAH48985.1; -; Genomic_DNA.
DR   RefSeq; WP_012687984.1; NC_012522.1.
DR   ProteinModelPortal; C1AT53; -.
DR   STRING; 632772.ROP_07380; -.
DR   EnsemblBacteria; BAH48985; BAH48985; ROP_07380.
DR   KEGG; rop:ROP_07380; -.
DR   PATRIC; fig|632772.20.peg.801; -.
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; UP000002212; Chromosome.
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; C1AT53.
DR   SWISS-2DPAGE; C1AT53.
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:UP000002212};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS00779198,
KW   ECO:0000313|EMBL:BAH48985.1};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS00779179}.
FT   ACT_SITE     53     53       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
FT   ACT_SITE     64     64       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
SQ   SEQUENCE   267 AA;  27686 MW;  092217D43DE4C75B CRC64;
     MSERLSRLAP TFAQCREEKR AALVGYLPAG FPTVPESIDV FKAMVESGCD IVEVGIAYSD
     PVMDGPTIQA AAETALQNGV RVRDVFTVVE AIASVGGKAV VMTYWNPVLQ YGVDKFARDL
     ASAGGLGLIT PNLIPEEAGE WIAASKEHDL DRIFLVAPSS TEERLAITLD ASSGFVYAAS
     TMGVTGARDA VSSMAPELTA RIRAHSDIPV GVGLGVRSGA QAAEIAAYAD AVIVGSALVT
     AAESGLDAVR SLTEELAEGV RSATVAS
//

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