(data stored in SCRATCH zone)

SWISSPROT: D6ZBW3_SEGRD

ID   D6ZBW3_SEGRD            Unreviewed;       262 AA.
AC   D6ZBW3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01103933};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01093371};
GN   Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131};
GN   OrderedLocusNames=Srot_0453 {ECO:0000313|EMBL:ADG96940.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96940.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96940.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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:SAAS01111173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
CC         D-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;
CC         EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131,
CC         ECO:0000256|SAAS:SAAS01126077};
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:SAAS01093362}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111165}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00131, ECO:0000256|RuleBase:RU003662,
CC       ECO:0000256|SAAS:SAAS01111172}.
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DR   EMBL; CP001958; ADG96940.1; -; Genomic_DNA.
DR   RefSeq; WP_013137396.1; NC_014168.1.
DR   STRING; 640132.Srot_0453; -.
DR   EnsemblBacteria; ADG96940; ADG96940; Srot_0453.
DR   KEGG; srt:Srot_0453; -.
DR   eggNOG; ENOG4105F6H; Bacteria.
DR   eggNOG; COG0159; LUCA.
DR   HOGENOM; HOG000223815; -.
DR   KO; K01695; -.
DR   OMA; DYPPEEC; -.
DR   OrthoDB; 912786at2; -.
DR   BioCyc; SROT640132:G1GLH-453-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002247; Chromosome.
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   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; D6ZBW3.
DR   SWISS-2DPAGE; D6ZBW3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093358};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093369};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01093361,
KW   ECO:0000313|EMBL:ADG96940.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093372}.
FT   ACT_SITE     52     52       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
FT   ACT_SITE     63     63       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
SQ   SEQUENCE   262 AA;  27450 MW;  04810F318EE543B7 CRC64;
     MSVPNSSADV IAACQAEGRA ALIGYLPAGY PDLKTSQRAF EILAEEGCDL LEIGVPYSDP
     VMDGPVIESA AVAALTAGFR LKDLFPLVEN LSKKDIPALV MTYWNPVFRY GVDRFADDLE
     NAGGLGLITP NLIPEEAEAW FQASDRLNLD RVFLVAPSST PERLILTTNS CRGFIYAAST
     MGVTGARNDV SMDAAELVAR VRKASGIAVG VGIGVSNGAA ARYVAGYADA VIVGSALVAA
     LGKGEDALRA LVRELAEGVR GN
//

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