ID TRPA_CORGL Reviewed; 280 AA.
AC P06562;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131};
GN OrderedLocusNames=Cgl3035, cg3364;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3808947; DOI=10.1093/nar/14.24.10113;
RA Matsui K., Sano K., Ohtsubo E.;
RT "Complete nucleotide and deduced amino acid sequences of the Brevibacterium
RT lactofermentum tryptophan operon.";
RL Nucleic Acids Res. 14:10113-10114(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-280.
RX PubMed=3609747; DOI=10.1016/0378-1119(87)90007-2;
RA Sano K., Matsui K.;
RT "Structure and function of the trp operon control regions of Brevibacterium
RT lactofermentum, a glutamic-acid-producing bacterium.";
RL Gene 53:191-200(1987).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; X04960; CAA28628.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00429.1; -; Genomic_DNA.
DR EMBL; BX927157; CAF18975.1; -; Genomic_DNA.
DR EMBL; AH003259; AAA83990.1; -; Genomic_DNA.
DR PIR; G24723; G24723.
DR RefSeq; NP_602228.1; NC_003450.3.
DR RefSeq; WP_004567954.1; NC_006958.1.
DR AlphaFoldDB; P06562; -.
DR SMR; P06562; -.
DR STRING; 196627.cg3364; -.
DR World-2DPAGE; 0001:P06562; -.
DR KEGG; cgb:cg3364; -.
DR KEGG; cgl:Cgl3035; -.
DR PATRIC; fig|196627.13.peg.2969; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_4_11; -.
DR OrthoDB; 9804578at2; -.
DR BioCyc; CORYNE:G18NG-12656-MONOMER; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; 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; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..280
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098773"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT CONFLICT 9..14
FT /note="ARLDTA -> GDASTRS (in Ref. 1; CAA28628)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="A -> R (in Ref. 1; CAA28628)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..144
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 273..280
FT /note="MKAATKKV -> TEGSDQEGLGL (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29075 MW; 5FA658D64A841AC5 CRC64;
MSRYDDLFAR LDTAGEGAFV PFIMLSDPSP EEAFQIISTA IEAGADALEL GVPFSDPVAD
GPTVAESHLR ALDGGATVDS ALEQIKRVRA AYPEVPIGML IYGNVPFTRG LDRFYQEFAE
AGADSILLPD VPVREGAPFS AAAAAAGIDP IYIAPANASE KTLEGVSAAS KGYIYAISRD
GVTGTERESS TDGLSAVVDN IKKFDGAPIL LGFGISSPQH VADAIAAGAS GAITGSAITK
IIASHCEGEH PNPSTIRDMD GLKKDLTEFI SAMKAATKKV
//
