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Database: UniProt
Entry: K1RUA8_9ZZZZ
LinkDB: K1RUA8_9ZZZZ
Original site: K1RUA8_9ZZZZ 
ID   K1RUA8_9ZZZZ            Unreviewed;       140 AA.
AC   K1RUA8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE            EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
DE   Flags: Fragment;
GN   ORFNames=LEA_17028 {ECO:0000313|EMBL:EKC52172.1};
OS   human gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC52172.1};
RN   [1] {ECO:0000313|EMBL:EKC52172.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA   Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA   Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA   Suarez A.;
RT   "Microbiota from the distal guts of lean and obese adolescents exhibit
RT   partial functional redundancy besides clear differences in community
RT   structure.";
RL   Environ. Microbiol. 15:211-226(2013).
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:0000256|ARBA:ARBA00000003};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011270}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKC52172.1}.
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DR   EMBL; AJWY01011650; EKC52172.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1RUA8; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR002028; Trp_synthase_suA.
DR   PANTHER; PTHR43406:SF1; TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKC52172.1"
SQ   SEQUENCE   140 AA;  15452 MW;  7E379A5EDA6DD142 CRC64;
     GVSGTIIPDL PFDDYLKVVK PIADKYDIRV IMMITPETSE ERIRFIDEHT DGFIYMVSSA
     SITGAQSSFG DAKLAYFNHI NSMNLRNPRM IGFGISNKQT LTSAQDNAAG AIIGSKFVTL
     LNETGDPDLA LDRLFECLKK
//
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