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Database: UniProt
Entry: F0VLC8_NEOCL
LinkDB: F0VLC8_NEOCL
Original site: F0VLC8_NEOCL 
ID   F0VLC8_NEOCL            Unreviewed;      1652 AA.
AC   F0VLC8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE            EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN   ORFNames=BN1204_053050 {ECO:0000313|EMBL:CEL69602.1}, NCLIV_053050
GN   {ECO:0000313|EMBL:CBZ54880.1};
OS   Neospora caninum (strain Liverpool).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ54880.1, ECO:0000313|Proteomes:UP000007494};
RN   [1] {ECO:0000313|EMBL:CBZ54880.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CBZ54880.1};
RA   Aslett M.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBZ54880.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CBZ54880.1};
RA   Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA   Wastling J.M., Pain A.;
RT   "Comparative genomics and transcriptomics of Neospora caninum and
RT   Toxoplasma gondii.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000007494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX   PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA   Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA   Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA   Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA   Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA   Wastling J.M.;
RT   "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT   Neospora caninum: Coccidia differing in host range and transmission
RT   strategy.";
RL   PLoS Pathog. 8:e1002567-e1002567(2012).
RN   [4] {ECO:0000313|EMBL:CEL69602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CEL69602.1};
RX   PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA   Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA   Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT   "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT   Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT   Transcript Features.";
RL   PLoS ONE 10:e0124473-e0124473(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00001633};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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DR   EMBL; FR823391; CBZ54880.1; -; Genomic_DNA.
DR   EMBL; LN714485; CEL69602.1; -; Genomic_DNA.
DR   RefSeq; XP_003884908.1; XM_003884859.1.
DR   GeneID; 13446584; -.
DR   VEuPathDB; ToxoDB:NCLIV_053050; -.
DR   eggNOG; KOG4201; Eukaryota.
DR   InParanoid; F0VLC8; -.
DR   OrthoDB; 230791at2759; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000007494; Chromosome X.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1652
FT                   /note="indole-3-glycerol-phosphate synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007655255"
FT   DOMAIN          261..509
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
FT   REGION          138..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1098..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1566..1600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1174..1207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1346..1362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1445..1474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1475..1501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1652 AA;  176356 MW;  6A40AFF70057D26B CRC64;
     MLAPARLLSR VPLLFFLLST AHHFAWRILA QRGEGIAFQT ARAATAARPS FLRCPQLQRC
     SSSRVFSPGP SYLAVVSPAS ASTLSLPSLA SFSSLRAPSR PRLPVERLPA PPANAPQALL
     CFLPGCTLHK SFLPLLPNVH GRNRQQSPND KSQERPASSP GASRLRASVR DRRLPSRALD
     QLQRLLEAKQ YEVKLLVEKH GSLLDPLALR QAYVHHTLNS KLTERMRIQT HVRERDEKIR
     AMHAARWQER DREAVLGKDA REEGQEPKCE QALQSHSHRV GGEHPRYDLQ EVLQEPETPH
     RLSVACDLKR RSCTNLAVDP RRLSYRNPGD VAVDCASAGA DVILVNTNKE GWGGSYEDLE
     ATTKALRNAY SWSERPAVVM KDIIIHPIQI AQAVEAKADG VYLHFCVAGK DLEDLLFACS
     TMGTQALVEV HSEAEAQQAE DAGATLLVVN QWDRYTGRLI PEHALRVRSV CSPEVIVLAS
     GGLTSTAQAT KCAKSGFDGV VLGQALTRPG ALDFIKELKA WQGAPRELVH LFAPDPRGAA
     AAARGLEEAA AAIEAEDAAL KAQREARRAA RPASRGPDSE TLPSEKREAL EQAALTSAHS
     KQFPRPEEAA LDAESEFPGD EGDLDVAEKV FEEAKRGWKP ETHAEPAETG GRQCSASDSV
     AGRPARDSGK ARKEATDRGH ARTRDRLSGG LSPDSTVPGE ERSEARGGQS RATPSDDFTE
     RVLRQSGPDF QPQPAESLFG PRAVPRRNGD ASQAPAHPSV NASSGSRDSG RSPSPASRGA
     YPAPPAGIVD VSGEQDEEPS QRLGQFHAFS TLRSSDASEG RDRRGDPPPV RIPEGTDCAP
     NEEQLLRACT RELLGQIARE QHVKRMADEE HRDLQLAMFR QYQRLARASP ADDQKARTGG
     AGPLFVPPLA LQDTLQTDPH FRSPGPEDAL DPLALGPQDA DSIAEPFKEA FPNDPARAAA
     ACTAAAAAAV ADPSGFAAVA RDHLQKAAER GAYTLADSND PAAALSAAAP TFAAASATAA
     LTAAVARGER DAQAAAKSAA AALRGAHPPS PKALAALAAA AVQERKARGD RPDQWGAPFG
     PTDEQARVVD AEPQLLGASL APRGAAGRQG EEARSRESCE SRDPTARREI GMVPFGGPDE
     EAELFDEAEL ERIGRLFFTE EELDGFLREL RAKKATRQSA RRGGEEEGVH GRAEKREDVH
     SRRQGFHTAQ RPDGGGEEAT QKGTAVDTAA GAGVRTGSGG SLPMCLGKPP ETENSREGQD
     ARADKEGTGT AEARTDGNGV PRRVQTETAG GAGAEASVEE RVADPARASE PSESSSESRP
     VRARPSKAAA SWQAEKVSFS TQEWFARANR RKKEDHELVQ HVRQQTQRAA DQPAGKRDGS
     PETDADSAPD SVSGARAETS SEAGASFRDG GRETFSRFGR HAPGPSLTTP MDQMEAFLPF
     FQGRGSHHHL EDPPEVQERM QQEAFLEELK RRESTGGLTS ATLTGNPADS PLGDPSRTGQ
     QAYELLEAQQ KRLQAERRQR PPAASLRAEA VAAAAAAAAA ALADGAPPQA AVQAVSRAAG
     AATVGSAVDL SSRDREKPAN GCRQSTAGET EESVQRADAA PRAAVQGAML GGERGAYAAL
     WGTSSQGAGG FFESYVDELA QSGGLQVEPS ED
//
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