ID H6C402_EXODN Unreviewed; 738 AA.
AC H6C402;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=HMPREF1120_06379 {ECO:0000313|EMBL:EHY58367.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY58367.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58367.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58367.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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; JH226134; EHY58367.1; -; Genomic_DNA.
DR RefSeq; XP_009158828.1; XM_009160580.1.
DR AlphaFoldDB; H6C402; -.
DR STRING; 858893.H6C402; -.
DR GeneID; 20311018; -.
DR VEuPathDB; FungiDB:HMPREF1120_06379; -.
DR eggNOG; KOG1395; Eukaryota.
DR eggNOG; KOG4175; Eukaryota.
DR HOGENOM; CLU_016734_1_2_1; -.
DR InParanoid; H6C402; -.
DR OMA; VDTARHS; -.
DR OrthoDB; 9569at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000007304; Unassembled WGS sequence.
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:UP000007304};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU003663}.
FT DOMAIN 390..712
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 738 AA; 79464 MW; 35F702C21CFBAB47 CRC64;
MEALKATFAR CKEENRPALV TYFTAGYPTK ESTPDVMLGL QAGGADIIEL GLPFTDPIAD
GPTIQKSNTI ALQNGVTVST ALEFVREARK RGLRVPVLFM GYYNPLLRYG EDRMLKDCRE
AGVNGFIMVD LPPEEAVRFR NNCAMAGLSY VPLIAPATSE KRMKLLCKIA DSFIYVVSRM
GVTGATGTLN TKLPELLERV HQYSGGVPAA VGFGVSTREH FLSVAEIAEG VVIGSQIVTV
LGNAKEGEYA KAVQEYCSQI TGRKVGEFNE TNGLTREVGI VETMNAAKEP NASTNGLNGH
QVQVDKVITD ADVPSEPGLA DQLDALNSET NGTEPNPNAI PARFGQFGGQ YVPESLMDCL
AELEEGFSKA KNDPEFWKEF RSYYPYMSRP SSLHLADRLT EKVGGAQIYL KREDLNHTGS
HKINNALGQI LVAKRLGKTR IIAETGAGQH GVATATVCAK FGMECVVYMG AEDVRRQALN
VFRMKLLGAK VVAVEAGSRT LRDAVNEALR AWVVDLDTTH YIIGSAIGPH PFPTIVRTFQ
SVIGQETKEQ MKELTGKLPD AVIACVGGGS NAVGMFFPFS SDPSVKLIGV EAAGEGVDTG
RHSATLSGGS VGVLHGVRTY VLQNEHGQIA DTHSISAGLD YPGVGPELSN WKDSQRAQFI
SATDAQALIG FRTLSETEGI IPALESSHAI YGAMEVAKKM SKDQTLVICL SGRGDKDVQS
VADELPRLGP QIGWELRF
//
