ID V9H028_ECOLX Unreviewed; 268 AA.
AC V9H028; A0A0J3VG66;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 ECO:0000313|EMBL:AAB60046.1};
GN ORFNames=BKL28_004435 {ECO:0000313|EMBL:EFH0045569.1}, C2R31_004687
GN {ECO:0000313|EMBL:EFA8786752.1}, CY655_08555
GN {ECO:0000313|EMBL:AZZ26105.1}, D9D43_16090
GN {ECO:0000313|EMBL:MGE15071.1}, F7N46_07820
GN {ECO:0000313|EMBL:EFE8673047.1}, F9B07_13455
GN {ECO:0000313|EMBL:MTE89831.1}, HJQ60_000653
GN {ECO:0000313|EMBL:HAI5330730.1}, HL563_09975
GN {ECO:0000313|EMBL:HAJ0834065.1}, NCTC12950_03037
GN {ECO:0000313|EMBL:STP51549.1}, NCTC9044_05610
GN {ECO:0000313|EMBL:VED14675.1}, NCTC9077_03479
GN {ECO:0000313|EMBL:STJ11755.1}, NCTC9702_03305
GN {ECO:0000313|EMBL:VED36045.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAB60046.1};
RN [1] {ECO:0000313|EMBL:AAB60046.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ECOR 50 {ECO:0000313|EMBL:AAB60046.1};
RX PubMed=8095913;
RA Milkman R., Bridges M.M.;
RT "Molecular evolution of the Escherichia coli chromosome. IV. Sequence
RT comparisons.";
RL Genetics 133:455-468(1993).
RN [2] {ECO:0000313|EMBL:AAB60046.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ECOR 50 {ECO:0000313|EMBL:AAB60046.1};
RA Milkman R.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAB60046.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ECOR 50 {ECO:0000313|EMBL:AAB60046.1};
RA Milkman R.;
RT "Recombinational exchange among clonal populations.";
RL (In) Neidhardt F.C. (eds.);
RL ESCHERICHIA COLI AND SALMONELLA. CELLULAR AND MOLECULAR BIOLOGY., pp.1-1,
RL American Society for Microbiology, Washington, DC (1996).
RN [4] {ECO:0000313|EMBL:AZZ26105.1, ECO:0000313|Proteomes:UP000284592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-1246 {ECO:0000313|EMBL:AZZ26105.1,
RC ECO:0000313|Proteomes:UP000284592};
RA Bikkarolla S.K., Nordberg V., Kabir M.H., Muller V., Fritzsche J.,
RA Ambjornsson T., Giske C.G., Naver L., Sandegren L., Westerlund F.;
RT "Combining optical DNA mapping and long-read sequencing for full genomic
RT characterization of plasmids in a nosocomial resistance outbreak.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAI5330730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMC_487 {ECO:0000313|EMBL:HAI5330730.1}, and EC00618
RC {ECO:0000313|EMBL:HAJ0834065.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [6] {ECO:0000313|Proteomes:UP000254495, ECO:0000313|Proteomes:UP000255454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12950 {ECO:0000313|EMBL:STP51549.1,
RC ECO:0000313|Proteomes:UP000255454}, and NCTC9077
RC {ECO:0000313|EMBL:STJ11755.1, ECO:0000313|Proteomes:UP000254495};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|Proteomes:UP000528199, ECO:0000313|Proteomes:UP000567387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PNUSAE004760 {ECO:0000313|EMBL:EFH0045569.1,
RC ECO:0000313|Proteomes:UP000528199}, and PNUSAE011918
RC {ECO:0000313|EMBL:EFA8786752.1, ECO:0000313|Proteomes:UP000567387};
RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance;
RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S.,
RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|Proteomes:UP000271797, ECO:0000313|Proteomes:UP000277930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC9044 {ECO:0000313|EMBL:VED14675.1,
RC ECO:0000313|Proteomes:UP000271797}, and NCTC9702
RC {ECO:0000313|EMBL:VED36045.1, ECO:0000313|Proteomes:UP000277930};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|EMBL:HAJ0834065.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AMC_487 {ECO:0000313|EMBL:HAI5330730.1}, and EC00618
RC {ECO:0000313|EMBL:HAJ0834065.1};
RG NCBI Pathogen Detection Project;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [10] {ECO:0000313|EMBL:EFE8673047.1, ECO:0000313|Proteomes:UP000533482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM N17EC0060 {ECO:0000313|EMBL:MGE15071.1,
RC ECO:0000313|Proteomes:UP000272336}, and FSIS11923834
RC {ECO:0000313|EMBL:EFE8673047.1, ECO:0000313|Proteomes:UP000533482};
RG NARMS: The National Antimicrobial Resistance Monitoring System;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [11] {ECO:0000313|EMBL:MTE89831.1, ECO:0000313|Proteomes:UP000486847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE161 {ECO:0000313|EMBL:MTE89831.1,
RC ECO:0000313|Proteomes:UP000486847};
RA Ghatak S., Milton A.P., Rhetso K., Purkait D., Das S., Puro K.-U.,
RA Shakuntala I., Sen A., Sanjukta R., Priya G.B., Mawlong M., Lyngdoh V.,
RA Rynghang J., Mawphlang B.L.;
RT "Comparative genomic analysis of antimicrobial resistant Escherichia coli
RT of diverse origin.";
RL Submitted (OCT-2019) 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 ---------------------------------------------------------------------------
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; U23497; AAB60046.1; -; Genomic_DNA.
DR EMBL; CP025573; AZZ26105.1; -; Genomic_DNA.
DR EMBL; AASCBU010000034; EFA8786752.1; -; Genomic_DNA.
DR EMBL; AASOHJ010000007; EFE8673047.1; -; Genomic_DNA.
DR EMBL; AASUOH010000043; EFH0045569.1; -; Genomic_DNA.
DR EMBL; DABERK010000002; HAI5330730.1; -; Genomic_DNA.
DR EMBL; DABGYN010000009; HAJ0834065.1; -; Genomic_DNA.
DR EMBL; RNLZ01000029; MGE15071.1; -; Genomic_DNA.
DR EMBL; WCEW01000013; MTE89831.1; -; Genomic_DNA.
DR EMBL; UGCU01000001; STJ11755.1; -; Genomic_DNA.
DR EMBL; UGFM01000001; STP51549.1; -; Genomic_DNA.
DR EMBL; LR134238; VED14675.1; -; Genomic_DNA.
DR EMBL; LR134246; VED36045.1; -; Genomic_DNA.
DR RefSeq; WP_000443071.1; NZ_WTVC01000005.1.
DR PATRIC; fig|562.7003.peg.4842; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000254495; Unassembled WGS sequence.
DR Proteomes; UP000255454; Unassembled WGS sequence.
DR Proteomes; UP000271797; Chromosome 1.
DR Proteomes; UP000272336; Unassembled WGS sequence.
DR Proteomes; UP000277930; Chromosome 1.
DR Proteomes; UP000284592; Chromosome.
DR Proteomes; UP000486847; Unassembled WGS sequence.
DR Proteomes; UP000528199; Unassembled WGS sequence.
DR Proteomes; UP000533482; Unassembled WGS sequence.
DR Proteomes; UP000567387; Unassembled WGS sequence.
DR Proteomes; UP000845800; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 268 AA; 28726 MW; 439232C8A06670AA CRC64;
MERYESLFAQ LKERKEGAFV PFVTLGDPGI EQSLKIIDTL IEAGADALEL GIPFSDPLAD
GPTIQNATLR AFAAGVTPAQ CFEMLALIRQ KHPTIPIGLL MYANLVFNKG IDEFYAQCEK
VGVDSVLVAD VPVEESAPFR QAALRHNVAP IFICPPNADD DLLRQIASYG RGYTYLLSRA
GVTGAENRAA LPLNHLVTKL KEYNAAPPLQ GFGISAPDQV KAAIDAGAAG AISGSAIVKI
IEQHINEPEK MLAALKAFVQ PMKAATRS
//
