ID R5SKC2_9FIRM Unreviewed; 257 AA.
AC R5SKC2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=BN540_00525 {ECO:0000313|EMBL:CCZ54270.1};
OS Dialister invisus CAG:218.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=1263072 {ECO:0000313|EMBL:CCZ54270.1, ECO:0000313|Proteomes:UP000017966};
RN [1] {ECO:0000313|EMBL:CCZ54270.1, ECO:0000313|Proteomes:UP000017966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:218 {ECO:0000313|Proteomes:UP000017966};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCZ54270.1}.
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DR EMBL; CBAF010000092; CCZ54270.1; -; Genomic_DNA.
DR AlphaFoldDB; R5SKC2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000017966; 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 Reference proteome {ECO:0000313|Proteomes:UP000017966};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 55
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 257 AA; 28202 MW; 282AF26A47CBBFC9 CRC64;
MSRIKEAFKN GKALIGFLTA GVPSAEDTLR YMGDLETAGA DLIEIGVPFS DPVADGAVIM
EADVQALKNK VHLPQVIEIV KAFRKQSETP VVFLTYYNPI FNYGVKKFFE EAKDIGLDGV
AIPDLPYEEQ MEIRPFADTY EIDIIQIIGP ASEERICQNV RNATGFIYIV SSTESANRKS
DMKTNLADII SVIRKTTDTP VVVGLDGHHT EELQGMKEMA DGITTGSIVV DMINKNGKEA
GAPIQEYVEK LKISIKG
//
