ID A0A178ALG7_9PLEO Unreviewed; 1591 AA.
AC A0A178ALG7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=IQ06DRAFT_226091 {ECO:0000313|EMBL:OAK98466.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98466.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK98466.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98466.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; KV441716; OAK98466.1; -; Genomic_DNA.
DR STRING; 765868.A0A178ALG7; -.
DR InParanoid; A0A178ALG7; -.
DR OrthoDB; 9569at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd01115; SLC13_permease; 1.
DR CDD; cd14478; SPX_PHO87_PHO90_like; 1.
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; IPR004680; Cit_transptr-like_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR004331; SPX_dom.
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; PF03600; CitMHS; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF03105; SPX; 2.
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; PS51382; SPX; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003663};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU003663}.
FT TRANSMEM 1128..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1159..1185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1261..1287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1337..1361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1381..1399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1406..1428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1434..1454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1475..1501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1521..1546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1567..1589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 743..1005
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REGION 779..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1591 AA; 174987 MW; 34F84F5EEED1BC3D CRC64;
MDAIKKTFAQ CKKEGRAALV TYVTAGYPTA QDTPDIMLGM EAGGADIIEL GMPFTDPIAD
GPTIQTANTQ ALKNGINTED VLQMIRDARK RGLKAPVMLM GYYNPLLSYG EERMLQDAKE
AGANGFIMVD LPPEEALRFR NFCRSYGLSY VPLIAPATSE HRMRVLCKIA DSFIYVVSRM
GVTGASGTMN AALPQLLERV HKYSGNIPAA VGFGVSTRDH FLSVGKIAEG VVIGSQIINT
IAKSEPGKCA KDVEQYCDQI CGKSSRATTR EVGIVETMSE AKEISGVHVD KVITDADTPD
GPGLADQLEA LNTEGSDGFD EDHAHPPRFG EFGGQYVPES LMDCLSELEK GFSKAVDDPK
FWEEYRSYYE YMGRPGHLHL AERLTEHAGG ANIWLKREDL NHTGSHKINN ALGQVLIARR
LGKTEIIAET GAGQHGVATA TVCAKFNMKC TIYMGAEDVR RQALNVFRIK LLGATVIAVE
AGSQTLRDAV NEALRAWVVH LDTTHYIIGS AIGPHPFPTI VRTFQSIIGN ETKEQMQEKR
GKLPDAVVAC VGGGSNAVGM FYPFSKDPSV KLLGVEAGGD GIDTDRHSAT LSAGTKGVLH
GVRTYILQNK HGQISDTHSV SAGLDYPGVG PELSSWKDSE RAKFIACTDA EAFIGFRLLS
QLEGIIPALE TSHAVFGALE LAKTMSKDQD IVICVSGRGD KDVQSVAEEL PKLGPKIGWD
LRCNKRDRKR REKLEQLREA DEMKFSHSLQ FNAVPDWSNH YIAYSNLKKQ IYSLETQINQ
KPEHTDPESS PLLNGDVDDP DKIFTNTLDA ELEKVTSFYQ IKENEIYEEL SAMLKDEDNY
DMETDGFEQE QAQMPPDQRL RKSSIFRQVG FTRPRALSGT SGQSTADGTL PDEDDSDEEA
NETSRLRRKS DDGRVRRSHT NENMAASTDY SASRRRTSAA FEDYNDMAFS ALYDEGVSLK
KRAVSVYVSL CELRSFIQLN KTGFEKVLKK YDKILDRKLK SFYLNKYVYP AHPFQQATMD
KLTQNLDQIE GAYAHLCTKG DVAEAKRELR LHLREHVVWE RNTVWREMIG IERKAQAANI
GITQTLLGRD RAGGKVRRQG DDVEPDIKEV STPIGKYRCP QWLISRTFWM LVACIAIFVV
LLVLPIMEKP EQQNCLAMVV FVSLLWATEA IPLFVTSLLV PFLAVTLDVV RSDDKPHQRL
DSKHAASYVF SAMWTPVIML LLGGFTIAAA LSKYNIAKMM ATFVLSKAGT KPRTVLLTNM
FVAMFASMWI SNVAAPVLCF SIIQPILRNL PADSDMTKAL LLGIALSSNI GGAASPIASP
QNLIALQNME PEPSWGVWFF VALPVCIISI LCIWGLLLVT FQPGRNTTIV PIRPLKDKFT
GVQWFISIVT VVTIVLWCVS HQLEPIFGDM GVVAIIPLVL FFGTGILTKE DFNNFLWTII
ILAAGGLALG KSVNSSGLLH TIAESITSGV EGMSLYSVMV VFAGLILVVA TFISHTVAAL
IVLPLVQQVG AQMEEPHPNL LVMGAVLMAS GAMGLPTSGF PNMTAIMMED QRTGQRYLEV
KHFLTRGIPA SIITFVVIIT VGYGLMLAVG F
//
