GenomeNet

Database: UniProt
Entry: A0A0N6ZYI0_9MICO
LinkDB: A0A0N6ZYI0_9MICO
Original site: A0A0N6ZYI0_9MICO 
ID   A0A0N6ZYI0_9MICO        Unreviewed;       267 AA.
AC   A0A0N6ZYI0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=NI26_08675 {ECO:0000313|EMBL:AIV40241.1};
OS   Curtobacterium sp. MR_MD2014.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV40241.1, ECO:0000313|Proteomes:UP000069933};
RN   [1] {ECO:0000313|Proteomes:UP000069933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA   Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA   Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA   Newman D.K.;
RT   "Isolation and characterization of species affiliated with family
RT   Actinomycetaceae.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AIV40241.1, ECO:0000313|Proteomes:UP000069933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV40241.1,
RC   ECO:0000313|Proteomes:UP000069933};
RX   PubMed=26722011;
RA   Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA   Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA   Newman D.K., Dawson S.C.;
RT   "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT   from Topsoil in Woods Hole, Massachusetts.";
RL   Genome Announc. 3:0-0(2015).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP009755; AIV40241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N6ZYI0; -.
DR   STRING; 1561023.NI26_08675; -.
DR   KEGG; cum:NI26_08675; -.
DR   PATRIC; fig|1561023.3.peg.1800; -.
DR   OrthoDB; 9804578at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000069933; 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:UP000069933};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00131}.
FT   ACT_SITE        55
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   267 AA;  27749 MW;  8646E1BA2609733D CRC64;
     MTNPGPSTSV ATTIDTANAE RAGAVVGYLP AGFPDLQTSV DAAVALAENG VDVIELGLPY
     SDPVMDGPVI QRAAEESLAN GFRVAQVFDA VDQITSRVDV PVLVMTYWNP VLRYGVDRFA
     DDLVAAGASG LITPDLIPDE GRAWIDASER TGLDRVFLAA PSSTDTRMEQ AVRSSRGFVY
     AVSTMGVTGA RVGVDTAART VVSRLRDAGV ERTCVGLGIS TADQVREVLE YADGAIVGSA
     FVRALADLGV QGVADRAADL TSGAARS
//
DBGET integrated database retrieval system