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TRPD_ACIAD
ID   TRPD_ACIAD              Reviewed;         349 AA.
AC   P00500; Q6F9N2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211};
DE            EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211};
GN   Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; OrderedLocusNames=ACIAD2462;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6599977; DOI=10.1093/oxfordjournals.molbev.a040331;
RA   Kaplan J.B., Goncharoff P., Seibold A.M., Nichols B.P.;
RT   "Nucleotide sequence of the Acinetobacter calcoaceticus trpGDC gene
RT   cluster.";
RL   Mol. Biol. Evol. 1:456-472(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
RA   Ponniah K., Nigon L.V., Anderson B.F., Norris G.E., Patrick W.M.;
RT   "Structure of anthranilate phosphoribosyl transferase from Acinetobacter
RT   baylyi.";
RL   Submitted (AUG-2012) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-
CC       phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-
CC       phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP-Rule:MF_00211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC         Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00211}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR   EMBL; M36636; AAA21904.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG69232.1; -; Genomic_DNA.
DR   PIR; A00585; NPKEDC.
DR   RefSeq; WP_004928448.1; NC_005966.1.
DR   PDB; 4GTN; X-ray; 2.03 A; A=2-349.
DR   PDB; 4YI7; X-ray; 1.85 A; A=2-349.
DR   PDBsum; 4GTN; -.
DR   PDBsum; 4YI7; -.
DR   AlphaFoldDB; P00500; -.
DR   SMR; P00500; -.
DR   STRING; 62977.ACIAD2462; -.
DR   EnsemblBacteria; CAG69232; CAG69232; ACIAD2462.
DR   GeneID; 45234767; -.
DR   KEGG; aci:ACIAD2462; -.
DR   eggNOG; COG0547; Bacteria.
DR   HOGENOM; CLU_034315_2_1_6; -.
DR   OMA; GPMTNPA; -.
DR   OrthoDB; 1238435at2; -.
DR   BioCyc; ASP62977:ACIAD_RS11250-MON; -.
DR   BRENDA; 4.1.3.27; 5690.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   HAMAP; MF_00211; TrpD; 1.
DR   InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   PANTHER; PTHR43285; PTHR43285; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   TIGRFAMs; TIGR01245; trpD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW   Transferase; Tryptophan biosynthesis.
FT   CHAIN           1..349
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_0000154417"
FT   BINDING         82
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         82
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         85..86
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         92..95
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         110..118
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         113
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         122
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         168
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   HELIX           2..11
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           18..29
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           35..48
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           52..64
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           93..103
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           123..128
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           165..171
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           176..180
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           202..211
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          215..222
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   TURN            263..265
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           270..281
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           287..306
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   STRAND          309..312
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           313..326
FT                   /evidence="ECO:0007829|PDB:4YI7"
FT   HELIX           328..343
FT                   /evidence="ECO:0007829|PDB:4YI7"
SQ   SEQUENCE   349 AA;  37556 MW;  AF53E46A63564A89 CRC64;
     MNIQQALNHI TKNIHLTQAQ MEDVMRSIMQ GEATEAQIGA LMMGLRMKGE SIDEITAAAR
     VMRELAIKID VSDIQYLVDI VGTGGDGQNL FNVSTASSFV IAAAGATIAK HGNRGVSSKS
     GSSDLLEQAG INLDLDMQQT ERCIREMGVG FLFAPNHHKA MKYAVGPRRE LGIRSIFNLL
     GPLTNPAGVK RFVIGVFSDE LCRPIAEVMK QLGAEHVMVV HSKDGLDEIS LASQTYIAEL
     KNGEVTEWVL NPEDVNIPSQ TLSGLIVEDS NASLKLIKDA LGRKKSDIGE KAANMIALNA
     GAGIYVSGLA TSYKQGVALA HDIIYGGQAL EKMSILSEFT KALKEYANN
 
 
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