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Database: UniProt
Entry: A0A0K9GSR1_9BACI
LinkDB: A0A0K9GSR1_9BACI
Original site: A0A0K9GSR1_9BACI 
ID   A0A0K9GSR1_9BACI        Unreviewed;       261 AA.
AC   A0A0K9GSR1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=AC625_07025 {ECO:0000313|EMBL:KMY49307.1};
OS   Peribacillus loiseleuriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY49307.1, ECO:0000313|Proteomes:UP000037146};
RN   [1] {ECO:0000313|Proteomes:UP000037146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) 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}.
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:KMY49307.1}.
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DR   EMBL; LFZW01000001; KMY49307.1; -; Genomic_DNA.
DR   RefSeq; WP_049680639.1; NZ_LFZW01000001.1.
DR   AlphaFoldDB; A0A0K9GSR1; -.
DR   STRING; 1679170.AC625_07025; -.
DR   PATRIC; fig|1679170.3.peg.1511; -.
DR   OrthoDB; 9804578at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000037146; Unassembled WGS sequence.
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:UP000037146};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00131}.
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   261 AA;  28365 MW;  931AF645823CFFCD CRC64;
     MGNKSLQDTL AELHVRQEKA FIPYIMAGDG GLDKLKEDLL RLQNAGATAV ELGVPFSDPV
     ADGPTIQLAG KRALAEGVTL KKIISKLIEI KDEVDIPIIF MAYLNSLLAY GIGNFSNDCV
     KAGVSGCIVP DLPIEEEEIL AQDLKNANIS LIRLVALTSS QERIEKIVEN AEGFIYAVTV
     TGITGVRESF EEEVGLYLNR IREASSIPVL AGFGISTPEH VERASLYCDG VIVGSKIIQS
     LQSENYREID ELILASKKVI Y
//
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