COAD1_ORYSJ
ID COAD1_ORYSJ Reviewed; 187 AA.
AC Q6ZLC4; A0A0P0X3F1;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Phosphopantetheine adenylyltransferase 1;
DE EC=2.7.7.3;
DE AltName: Full=Dephospho-CoA pyrophosphorylase 1;
DE AltName: Full=Pantetheine-phosphate adenylyltransferase 1;
GN OrderedLocusNames=Os07g0179400, LOC_Os07g08210; ORFNames=OJ1014_E09.9;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC Does not accept 4'-phosphopantothenoylcysteine as a substrate (By
CC similarity). {ECO:0000250}.
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;
CC -!- ACTIVITY REGULATION: Inhibited by CoA. {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5.
CC -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000305}.
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DR EMBL; AP003800; BAC83033.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20949.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00308.1; -; Genomic_DNA.
DR EMBL; AK073022; BAG93250.1; -; mRNA.
DR RefSeq; XP_015647028.1; XM_015791542.1.
DR AlphaFoldDB; Q6ZLC4; -.
DR SMR; Q6ZLC4; -.
DR STRING; 4530.OS07T0179400-01; -.
DR PaxDb; Q6ZLC4; -.
DR PRIDE; Q6ZLC4; -.
DR EnsemblPlants; Os07t0179400-01; Os07t0179400-01; Os07g0179400.
DR GeneID; 4342557; -.
DR Gramene; Os07t0179400-01; Os07t0179400-01; Os07g0179400.
DR KEGG; osa:4342557; -.
DR eggNOG; KOG3351; Eukaryota.
DR HOGENOM; CLU_035272_4_2_1; -.
DR InParanoid; Q6ZLC4; -.
DR OMA; PIHNGHR; -.
DR OrthoDB; 1543581at2759; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q6ZLC4; OS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coenzyme A biosynthesis; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..187
FT /note="Phosphopantetheine adenylyltransferase 1"
FT /id="PRO_0000429411"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 20038 MW; 94473B05F0474AE6 CRC64;
MITPPVAGDT FAGAPPPPSQ EEDAPPYGSV VLGGTFDRLH DGHRRLLKAS ADLARDRIVV
GVCTGPMLAK KEYAELIEPV EKRMKAVEDY IKSVKPELVV QVEPIEDPYG PSIIDDKLDA
IIVSKETLNG GFAVNRKREE KGLPLLKVEV VDLLSGGAEG EKLSSSALRK LEAEKANQQE
GAASKGV