ID B3DS09_BIFLD Unreviewed; 289 AA.
AC B3DS09;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
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:ACD97928.1};
GN OrderedLocusNames=BLD_0482 {ECO:0000313|EMBL:ACD97928.1};
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD97928.1, ECO:0000313|Proteomes:UP000002419};
RN [1] {ECO:0000313|EMBL:ACD97928.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD97928.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA Lee J.H., O'Sullivan D.J.;
RT "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT DJO10A and construction of a shuttle cloning vector.";
RL Appl. Environ. Microbiol. 72:527-535(2006).
RN [2] {ECO:0000313|EMBL:ACD97928.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD97928.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
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; CP000605; ACD97928.1; -; Genomic_DNA.
DR RefSeq; WP_010080646.1; NZ_AABM02000001.1.
DR AlphaFoldDB; B3DS09; -.
DR KEGG; blj:BLD_0482; -.
DR HOGENOM; CLU_016734_0_0_11; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002419; 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 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 289 AA; 30730 MW; DC91B42BDAE1F84F CRC64;
MTNEATTPSG QPLGISHKPS KSVAMFTKFK AENKPAFIGY LPYGFPNPDV SLDAFKTMVE
HGVDAVEIGL PYSDPVMDGP VIQAAASIAL NNGETIKRVF EAVETVANAG GVPLIMSYWN
LVYHYGVERF ARDFENAGGA GLITPDLIPD EAGEWIEASD RHGLDRIFLV SPDSSTERLE
TVARNARGFV YAAARMGVTG ERATIDASPE LLVERTRQAG AENVCVGIGV STAEQGAKVG
SYADGVIVGS ALVHTLLADD NKTARDPKEG LKLLAAKSEE LAEGIHNAR
//
