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Database: UniProt
Entry: K9VSG5_9CYAN
LinkDB: K9VSG5_9CYAN
Original site: K9VSG5_9CYAN 
ID   K9VSG5_9CYAN            Unreviewed;       265 AA.
AC   K9VSG5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131};
GN   Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131};
GN   ORFNames=Osc7112_5960 {ECO:0000313|EMBL:AFZ10155.1};
OS   Oscillatoria nigro-viridis PCC 7112.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ10155.1, ECO:0000313|Proteomes:UP000010478};
RN   [1] {ECO:0000313|EMBL:AFZ10155.1, ECO:0000313|Proteomes:UP000010478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ10155.1,
RC   ECO:0000313|Proteomes:UP000010478};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC       indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00131}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00131};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC       ECO:0000256|HAMAP-Rule:MF_00131}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00131}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00131, ECO:0000256|RuleBase:RU003662}.
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DR   EMBL; CP003614; AFZ10155.1; -; Genomic_DNA.
DR   RefSeq; WP_015179356.1; NC_019729.1.
DR   AlphaFoldDB; K9VSG5; -.
DR   STRING; 179408.Osc7112_5960; -.
DR   KEGG; oni:Osc7112_5960; -.
DR   PATRIC; fig|179408.3.peg.7432; -.
DR   eggNOG; COG0159; Bacteria.
DR   HOGENOM; CLU_016734_0_2_3; -.
DR   OrthoDB; 9804578at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000010478; 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; Aldolase class I; 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   NCBIfam; TIGR00262; trpA; 1.
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.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00131};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00131};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00131};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00131}.
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT   ACT_SITE        59
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   265 AA;  28457 MW;  7D05856A5C4F898C CRC64;
     MTISNCFETL RKNHQCALIP FITAGDPDLE TTAKALQILD DNGADAIELG VPYSDPLADG
     PVIQAAATRA LQRGTRLDAV LEMVAKVSPN LRSPIILFTY YNPILYRGIE TFLQQIKSAG
     VQGLVVPDLP LEEADSLIQP ANKLGIELTL LVAPTSPKSR IEAIARQSQG FIYLVSVTGV
     TGVREGLETR AKELLQELRA VTDKPIGVGF GISQPEHARQ VKEWGADAAI VGSAFVKRLA
     QGTPEQGLEA IGEFCKSLKT AIQNA
//
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