ID A0A117DVI3_ASPNG Unreviewed; 722 AA.
AC A0A117DVI3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ABL_01002 {ECO:0000313|EMBL:GAQ35013.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ35013.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ35013.1}.
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DR EMBL; BCMY01000001; GAQ35013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117DVI3; -.
DR PaxDb; 5061-CADANGAP00001678; -.
DR VEuPathDB; FungiDB:An02g02170; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1105787; -.
DR VEuPathDB; FungiDB:ATCC64974_60670; -.
DR VEuPathDB; FungiDB:M747DRAFT_291920; -.
DR OMA; VDTARHS; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000068243; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU003663}.
FT DOMAIN 374..696
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 722 AA; 77262 MW; 6AB7B1EC88927BD6 CRC64;
MDGIKNAFAR AKQEKRAALV AYFTAGYPTV EETVDVLMGL ENGGADIIEM GVPFTDPIAD
GPTIQKANTQ ALANGVTIPL VLDQVRTARS RGLRAPVLLM GYYNPLMQYG EELMLQHCKD
AGVNGFIMVD LPPEEAVRFR DLCASAGLSY VPLIAPATSE SRMKLLCKIA DSFIYVVSRM
GVTGATGKLS SNLPDLLSRV HTWSGNVPTA LGFGVSTREH FLSVQNISEG VVIGSQIITV
LGDAPAGQAA KHAQDYLSSV TGRRLERDAQ GKVTGSVNVL DPVLKEAPPA LSQPTDVITN
DDTPAGPGLV DQIEALNGSG DPALIPSRFG EFGGQYVPES LMDCLAELER GFDQARNDPK
FWEEYRSYYP YMGRPSSLHL ADRLTEHVGG ANIWLKREDL NHTGSHKINN ALGQILLARR
LGKKRIIAET GAGQHGVATA TVCAKFGMEC VVYMGAEDVR RQALNVFRMR LLGASVVAVD
AGSRTLRDAV NEALRAWVVH LDTTHYIIGS AIGPHPFPTI VRTFQSVIGD ETKEQMKALI
GKLPDAVVAC VGGGSNAVGM FYPFSNDPSV KLLGVEAGGD GVDTDRHSAT LSGGSKGVFH
GVRTYVLQDK HGQISETHSI SAGLDYPGVG PELSNWKDSD RAKFIAATDA EALTGFRALA
QTEGIIPALE SSHAVFGAME LAKSMKTGDI VLNLSGRGDK DVQSVADELP RLGPKIGWDL
RF
//
