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TRPC_MYCTU
ID   TRPC_MYCTU              Reviewed;         272 AA.
AC   P9WFX7; L0T8S6; O06129; P0A632;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Indole-3-glycerol phosphate synthase;
DE            Short=IGPS;
DE            EC=4.1.1.48;
GN   Name=trpC; OrderedLocusNames=Rv1611; ORFNames=MTCY01B2.03;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44375.1; -; Genomic_DNA.
DR   PIR; A70557; A70557.
DR   RefSeq; NP_216127.1; NC_000962.3.
DR   RefSeq; WP_003407990.1; NZ_NVQJ01000016.1.
DR   PDB; 3QJA; X-ray; 1.29 A; A=1-272.
DR   PDB; 3T40; X-ray; 1.75 A; A=1-272.
DR   PDB; 3T44; X-ray; 1.60 A; A=1-272.
DR   PDB; 3T55; X-ray; 2.06 A; A=1-272.
DR   PDB; 3T78; X-ray; 1.60 A; A=1-272.
DR   PDB; 4FB7; X-ray; 1.30 A; A=1-272.
DR   PDBsum; 3QJA; -.
DR   PDBsum; 3T40; -.
DR   PDBsum; 3T44; -.
DR   PDBsum; 3T55; -.
DR   PDBsum; 3T78; -.
DR   PDBsum; 4FB7; -.
DR   AlphaFoldDB; P9WFX7; -.
DR   SMR; P9WFX7; -.
DR   STRING; 83332.Rv1611; -.
DR   PaxDb; P9WFX7; -.
DR   DNASU; 885294; -.
DR   GeneID; 885294; -.
DR   KEGG; mtu:Rv1611; -.
DR   TubercuList; Rv1611; -.
DR   eggNOG; COG0134; Bacteria.
DR   OMA; RGPHDLI; -.
DR   PhylomeDB; P9WFX7; -.
DR   BRENDA; 4.1.1.48; 3445.
DR   SABIO-RK; P9WFX7; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IDA:MTBBASE.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR   GO; GO:0046391; P:5-phosphoribose 1-diphosphate metabolic process; IDA:MTBBASE.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IDA:MTBBASE.
DR   CDD; cd00331; IGPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00134_B; IGPS_B; 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; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Decarboxylase; Lyase; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..272
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_0000154234"
FT   HELIX           5..22
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           27..36
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           43..47
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:3T44"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:4FB7"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           98..111
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          137..142
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           148..160
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          164..171
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           172..181
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          184..191
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   TURN            193..195
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           202..206
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          214..220
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           225..233
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   HELIX           251..259
FT                   /evidence="ECO:0007829|PDB:3QJA"
FT   TURN            260..263
FT                   /evidence="ECO:0007829|PDB:3QJA"
SQ   SEQUENCE   272 AA;  28023 MW;  9CA29D0F0FAC76C2 CRC64;
     MSPATVLDSI LEGVRADVAA REASVSLSEI KAAAAAAPPP LDVMAALREP GIGVIAEVKR
     ASPSAGALAT IADPAKLAQA YQDGGARIVS VVTEQRRFQG SLDDLDAVRA SVSIPVLRKD
     FVVQPYQIHE ARAHGADMLL LIVAALEQSV LVSMLDRTES LGMTALVEVH TEQEADRALK
     AGAKVIGVNA RDLMTLDVDR DCFARIAPGL PSSVIRIAES GVRGTADLLA YAGAGADAVL
     VGEGLVTSGD PRAAVADLVT AGTHPSCPKP AR
 
 
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