ID G8BHI8_CANPC Unreviewed; 711 AA.
AC G8BHI8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Tryptophan synthase {ECO:0000256|ARBA:ARBA00018724, ECO:0000256|RuleBase:RU003663};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043, ECO:0000256|RuleBase:RU003663};
GN Name=TRP5 {ECO:0000313|CGD:CAL0000154787};
GN OrderedLocusNames=CPAR2_501390 {ECO:0000313|CGD:CAL0000154787,
GN ECO:0000313|EMBL:CCE43913.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE43913.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
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).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
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 ECO:0000256|RuleBase:RU003663};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003663};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|RuleBase:RU003663}.
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; HE605207; CCE43913.1; -; Genomic_DNA.
DR AlphaFoldDB; G8BHI8; -.
DR STRING; 578454.G8BHI8; -.
DR EnsemblFungi; CPAR2_501390-T; CPAR2_501390-T-p1; CPAR2_501390.
DR CGD; CAL0000154787; TRP5.
DR VEuPathDB; FungiDB:CPAR2_501390; -.
DR eggNOG; KOG1395; Eukaryota.
DR eggNOG; KOG4175; Eukaryota.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000005221; Chromosome 5.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR CDD; cd06446; Trp-synth_B; 1.
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 HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
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 NCBIfam; TIGR00263; trpB; 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 ECO:0000256|RuleBase:RU003663};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU003663};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003663};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003663};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU003663}.
FT DOMAIN 350..675
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 270..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 76606 MW; 9C85B6C2E9B51ACB CRC64;
MSSALKETFA RCKRENRNAL VNFITAGYPT IEDTVPILTN MQKAGVDIIE IGIPFSDPIA
DGPTIQTANI KALENGMTVA KVLDSVKQAR SAGVSVPLIL MGYYNPILKY GESQFLQDAA
SAGVNGFIIV DLPPEEAVKF RHACSKHGLS YVPLVAPATT DERLKVLGQI ADSFVYVVSK
MGTTGASNKV SAGIEELCAR VRKYIGQDTP IAVGFGVSTR EHFLAVGKVA DGVVIGSKIV
TLIGESKPGE RGETAYKYVR SILGDDYNAT APEQFQNGNK VDKEEGGDLT SQQPDFQESH
KYNPRFGDFG GQYVPEALHT CLAELEKGFE EAVADPQFWK EFKDLYSYIG RPSSLHKAER
LTEHAGGATI WLKREDLNHT GSHKINNALA QVLIAKRLGK KKIIAETGAG QHGVATATAC
AKFGLECTVF MGAEDTRRQA LNVFRMKILG ANVVPVKNGT QTLRDATSEA FRFWVSNLET
THYVVGSAIG PHPYPTLVRT FQSVIGQEVK QQFAELNNGK LPNAVVACVG GGSNSTGLFS
PFEKDLDVKM LGVEAGGDGI DTDRHSATLT AGLPGVFHGV RTFVLQDDDG QVHDTHSVSA
GLDYPGVGPE LAYWKSTGRA DFIAATDAQA LQGFKLLSQL EGIIPALESS HAIYGGVELA
KTLPQDQHIV INVSGRGDKD VQSVAEVLPK LGEEIGWDLR FEEDPSKKNV L
//
