ID A5DNH7_PICGU Unreviewed; 472 AA.
AC A5DNH7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Tryptophan synthase {ECO:0000256|ARBA:ARBA00018724};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
DE Flags: Fragment;
GN ORFNames=PGUG_04828 {ECO:0000313|EMBL:EDK40730.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40730.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40730.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpB family.
CC {ECO:0000256|ARBA:ARBA00005761}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpA family.
CC {ECO:0000256|ARBA:ARBA00006095}.
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DR EMBL; CH408160; EDK40730.2; -; Genomic_DNA.
DR RefSeq; XP_001482873.1; XM_001482823.1.
DR AlphaFoldDB; A5DNH7; -.
DR STRING; 294746.A5DNH7; -.
DR GeneID; 5124533; -.
DR KEGG; pgu:PGUG_04828; -.
DR VEuPathDB; FungiDB:PGUG_04828; -.
DR eggNOG; KOG1395; Eukaryota.
DR eggNOG; KOG4175; Eukaryota.
DR HOGENOM; CLU_016734_2_0_1; -.
DR InParanoid; A5DNH7; -.
DR OMA; NGGADMI; -.
DR OrthoDB; 9569at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.40.50.1100; -; 2.
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; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00262; trpA; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 341..457
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT NON_TER 472
FT /evidence="ECO:0000313|EMBL:EDK40730.2"
SQ SEQUENCE 472 AA; 51233 MW; CEF7CA5B1C3AFE1B CRC64;
MSAAIKETFA RCKKEGRNAL VNFITAGFPT IPDTVPIMLA MQKGGVDIIE LGIPFSDPIA
DGPTIQIANT KALENGITVP KCLELVKEAR AAGVTVPIIL MGYYNPILKY GEQKMIKDSA
AAGANGYIVV DLPPEDAVQF RASCATHGLS YVPLVAPATT DKRLKVLGSI ADSFIYVVSR
MGTTGALKSV AKGIDELCQR VRKFAGDTPL AVGFGVSTRD HFLTVGEAAD GVVIGSKIIT
LISEAAPEDR ADTAYRFVRS ILGDDYESKT HEFIAATPSE TKQAQLPEEE HKYNPRFGDF
GGQYVPEALH ACLAELERGF EDAVADPKFW EEFRSLYSYI GRPSSLHRAD RLTEYAGGAQ
IWLKREDLNH TGSHKINNAL AQVLIAKRLG KKKIIAETGA GQHGVATATA CAKFGLECQV
FMGAEDVRRQ ALNVFRMRIL GAKVNAVRNG TQTLRDATSE AFRYWVSNLE TT
//
