ID A0A099NZ13_PICKU Unreviewed; 700 AA.
AC A0A099NZ13;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=BOH78_2178 {ECO:0000313|EMBL:ONH74905.1}, C5L36_0B03480
GN {ECO:0000313|EMBL:AWU75097.1}, CAS74_003451
GN {ECO:0000313|EMBL:OUT21335.1}, JL09_g2800
GN {ECO:0000313|EMBL:KGK38043.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK38043.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
RN [2] {ECO:0000313|EMBL:KGK38043.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|EMBL:KGK38043.1};
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for Succinic Acid Production.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000189274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|Proteomes:UP000189274};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [4] {ECO:0000313|EMBL:ONH74905.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|EMBL:ONH74905.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:OUT21335.1, ECO:0000313|Proteomes:UP000195871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ckrusei653 {ECO:0000313|EMBL:OUT21335.1,
RC ECO:0000313|Proteomes:UP000195871};
RA Cuomo C., Forche A., Young S., Abouelleil A., Cao P., Chapman S.,
RA Cusick C., Shea T., Nusbaum C., Birren B.;
RT "The Genome Sequence of Candida krusei Ckrusei653.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AWU75097.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU75097.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; CP028774; AWU75097.1; -; Genomic_DNA.
DR EMBL; JQFK01000025; KGK38043.1; -; Genomic_DNA.
DR EMBL; MQVM01000008; ONH74905.1; -; Genomic_DNA.
DR EMBL; NHMM01000005; OUT21335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099NZ13; -.
DR STRING; 4909.A0A099NZ13; -.
DR VEuPathDB; FungiDB:C5L36_0B03480; -.
DR eggNOG; KOG1395; Eukaryota.
DR eggNOG; KOG4175; Eukaryota.
DR HOGENOM; CLU_016734_2_1_1; -.
DR OrthoDB; 9569at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR Proteomes; UP000189274; Unassembled WGS sequence.
DR Proteomes; UP000195871; Unassembled WGS sequence.
DR Proteomes; UP000249293; Chromosome 2.
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:UP000249293};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU003663}.
FT DOMAIN 342..666
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 700 AA; 75302 MW; 2B252CEAB5AA6B72 CRC64;
MSSHLRSAFV KAKEQGRNAL VTFITAYYPT PQDTIDILKG LQNGGADVIE LGIPFSDPIA
DGPTIQVANT KAIENGCTVQ TCIDLVRRAR EEGVTIPIVL MGYYNPILKY GEEKMVEASR
NAGANGFIVV DLPPEEAVKF RNICSTHEMS YIPLVAPSTT DDRLKLLAEI ADSFIYVVSR
MGSTGASITV TDSVGPLCDH IRKFTGNTPL AVGFGISTRQ HYLNVGKHSD GVVIGSKILS
LISDAPAGAR GKAAEDYVKS ILNGDGENTF ADSKIGLSTN VVENPDFTES HKHNPNFGNF
GGQYVPEALH ACLRELEVAF EDAIADPVFW EEFHSLYDYI GRPSTLHKAE RLSEYAGGAQ
IWLKREDLNH TGSHKINNAL AQILIAKRQG KTNIIAETGA GQHGVATATA CAKFGMTCTV
YMGAEDVRRQ ALNVFRMRIL GAKVVAVENG TKTLRDATSE AFRSWVTNLK TTYYVVGSAI
GPHPYPTLVR TFQSVIGNEI KKQFAEKNNG KLPNLVVACV GGGSNSTGTF SPFENDTQVK
LLGCEAGGSG VDTNHHSATL TVGEPGVFHG VKTYVLQDED GQVHDTHSVS AGLDYPGVGP
ELAAWKDSGR VEFIAVTDDQ ALEGFRLLSQ YEGIIPALES SHAIYGAVEA AKKMDKNQHV
VITVSGRGDK DVQSVAEVLP VLGPKIGWDL RFESGSDASK
//
