ID Q2IGW2_ANADE Unreviewed; 285 AA.
AC Q2IGW2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 124.
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=Adeh_4058 {ECO:0000313|EMBL:ABC83822.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC83822.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|EMBL:ABC83822.1, ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|EMBL:ABC83822.1,
RC ECO:0000313|Proteomes:UP000001935};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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}.
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DR EMBL; CP000251; ABC83822.1; -; Genomic_DNA.
DR RefSeq; WP_011423104.1; NC_007760.1.
DR AlphaFoldDB; Q2IGW2; -.
DR STRING; 290397.Adeh_4058; -.
DR KEGG; ade:Adeh_4058; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_7; -.
DR OrthoDB; 9804578at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001935; 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:UP000001935};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 80
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 285 AA; 29311 MW; 68677C47D575844C CRC64;
MSPRTARKPR AAAAPAAAER PDRITAAFER CRAERRAALV TYVMGGDPDL ATARDMALAC
VEGGADLVEL GVPFSDPIAD GPTIQAAAQR ALGAGTTLED VLGIAAAVRA RSQVPIALMG
YLNPMLAGGV ERLVRGCADA GVDALIIPDL LPEEAEVLAP AAAEAGVKLV YLLAPTSNPA
RVEAAVRAAT GFLYFVSVTG VTGARHAVAD EIAPLVSAVR SRTELPVVIG FGVATPEQAR
ALGPLADGVV VGSAIVKRIA EGGSRRARAE RVKRFVRSLG RALGR
//
