(data stored in ACNUC7421 zone)

SWISSPROT: COAD_RHILO

ID   COAD_RHILO              Reviewed;         166 AA.
AC   Q98M51;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
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};
DE            Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; OrderedLocusNames=mll0730;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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=ATP + D-pantetheine 4'-phosphate + 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00151}.
DR   EMBL; BA000012; BAB48262.1; -; Genomic_DNA.
DR   RefSeq; WP_010909617.1; NC_002678.2.
DR   SMR; Q98M51; -.
DR   STRING; 266835.14021650; -.
DR   EnsemblBacteria; BAB48262; BAB48262; BAB48262.
DR   KEGG; mlo:mll0730; -.
DR   eggNOG; ENOG4108ZEF; Bacteria.
DR   eggNOG; COG0669; LUCA.
DR   HOGENOM; HOG000006518; -.
DR   KO; K00954; -.
DR   OMA; EFQMALM; -.
DR   OrthoDB; 1846503at2; -.
DR   BioCyc; MLOT266835:G1G20-600-MONOMER; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000000552; Chromosome.
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   3: Inferred from homology;
DR   PRODOM; Q98M51.
DR   SWISS-2DPAGE; Q98M51.
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..166
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156262"
FT   NP_BIND         11..12
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   NP_BIND         95..97
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   NP_BIND         130..136
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         11
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         19
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         43
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         80
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         94
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         105
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   SITE            19
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
SQ   SEQUENCE   166 AA;  17738 MW;  06CB9C9FD1BD469B CRC64;
     MIERTALYAG SFDPLTNGHL DVLKASLAVA DIVYAAIGIH PGKKPLFSFE ERVQLIEDAT
     KAEFGRDGAR IKVVAFDGLV IDAARKQGAS IMIRGLRDGT DLDYEMQMAG MNETMAPELQ
     TVFLPASPSV RTITATLVRQ IASMGGDIRP FVPAAVAGAL TAKFAK
//

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