ID D5VR01_METIM Unreviewed; 272 AA.
AC D5VR01;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=Metin_0334 {ECO:0000313|EMBL:ADG13004.1};
OS Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13004.1, ECO:0000313|Proteomes:UP000002061};
RN [1] {ECO:0000313|EMBL:ADG13004.1, ECO:0000313|Proteomes:UP000002061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanocaldococcus infernus ME.";
RL Submitted (APR-2010) 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|ARBA:ARBA00003365, 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; CP002009; ADG13004.1; -; Genomic_DNA.
DR RefSeq; WP_013099750.1; NC_014122.1.
DR AlphaFoldDB; D5VR01; -.
DR STRING; 573063.Metin_0334; -.
DR GeneID; 9131336; -.
DR KEGG; mif:Metin_0334; -.
DR eggNOG; arCOG01086; Archaea.
DR HOGENOM; CLU_016734_0_2_2; -.
DR OrthoDB; 25658at2157; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002061; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 272 AA; 30505 MW; 7844101A4AC0BCDD CRC64;
MRIEEKFKEL KEKGEKAFIA FYVGGDPSYE VSLEALKRIC KYSDIVEIGI PFSDPVADGL
TIQKADIRAL NAGMTPIKAF KLVEELNKFY PDVPKVFLTY YNIIFKMGEE EFVKRCKEAG
VAGIIVPDLP IEEANSLHEI CEKYGVSLIF LVAPTTPDER IKKIVEKGSG FIYVVSTTGI
TGEREKLAKE AKETVERVKR YTDLPVCVGF GISKKEHVEE ICKVADGAIV GSAIVKIVEK
NLNDKEKMLK EIEDFVKELK EGTKKKLLNK VS
//
