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COAD_BURP1
ID   COAD_BURP1              Reviewed;         166 AA.
AC   Q3JW91;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
DE            EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
DE            Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
GN   OrderedLocusNames=BURPS1710b_0748;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH 3'-DEPHOSPHO-COA;
RP   4'-DIPHOSPHOPANTETHEINE AND ADENINE, AND SUBUNIT.
RC   STRAIN=1710b;
RX   PubMed=21904046; DOI=10.1107/s1744309111004349;
RA   Edwards T.E., Leibly D.J., Bhandari J., Statnekov J.B., Phan I.,
RA   Dieterich S.H., Abendroth J., Staker B.L., Van Voorhis W.C., Myler P.J.,
RA   Stewart L.J.;
RT   "Structures of phosphopantetheine adenylyltransferase from Burkholderia
RT   pseudomallei.";
RL   Acta Crystallogr. F 67:1032-1037(2011).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC         diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00151};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00151};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151,
CC       ECO:0000269|PubMed:21904046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00151}.
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DR   EMBL; CP000124; ABA49742.1; -; Genomic_DNA.
DR   RefSeq; WP_004195249.1; NC_007434.1.
DR   PDB; 3K9W; X-ray; 1.60 A; A=1-166.
DR   PDB; 3PXU; X-ray; 2.10 A; A=1-166.
DR   PDBsum; 3K9W; -.
DR   PDBsum; 3PXU; -.
DR   AlphaFoldDB; Q3JW91; -.
DR   SMR; Q3JW91; -.
DR   EnsemblBacteria; ABA49742; ABA49742; BURPS1710b_0748.
DR   GeneID; 56593817; -.
DR   GeneID; 66545995; -.
DR   KEGG; bpm:BURPS1710b_0748; -.
DR   HOGENOM; CLU_100149_0_1_4; -.
DR   OMA; EFQMALM; -.
DR   OrthoDB; 1846503at2; -.
DR   BRENDA; 2.7.7.3; 1031.
DR   UniPathway; UPA00241; UER00355.
DR   EvolutionaryTrace; Q3JW91; -.
DR   Proteomes; UP000002700; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02163; PPAT; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00151; PPAT_bact; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR001980; PPAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   PRINTS; PR01020; LPSBIOSNTHSS.
DR   TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..166
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_1000011110"
FT   BINDING         6..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:21904046,
FT                   ECO:0007744|PDB:3PXU"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W,
FT                   ECO:0007744|PDB:3PXU"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W,
FT                   ECO:0007744|PDB:3PXU"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W,
FT                   ECO:0007744|PDB:3PXU"
FT   BINDING         88..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU"
FT   BINDING         98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU"
FT   BINDING         123..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT                   ECO:0000305|PubMed:21904046"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           15..27
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           47..58
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           95..108
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   STRAND          113..117
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:3K9W"
FT   HELIX           147..160
FT                   /evidence="ECO:0007829|PDB:3K9W"
SQ   SEQUENCE   166 AA;  18530 MW;  C9CDDE2E32564B58 CRC64;
     MVVAVYPGTF DPLTRGHEDL VRRASSIFDT LVVGVADSRA KKPFFSLEER LKIANEVLGH
     YPNVKVMGFT GLLKDFVRAN DARVIVRGLR AVSDFEYEFQ MAGMNRYLLP DVETMFMTPS
     DQYQFISGTI VREIAQLGGD VSKFVFPSVE KWLTEKVAAM AQGPSA
 
 
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