ID A9A4T6_NITMS Unreviewed; 158 AA.
AC A9A4T6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00647};
DE EC=2.7.7.3 {ECO:0000256|HAMAP-Rule:MF_00647};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00647};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00647};
DE Short=PPAT {ECO:0000256|HAMAP-Rule:MF_00647};
GN Name=coaD {ECO:0000256|HAMAP-Rule:MF_00647};
GN OrderedLocusNames=Nmar_1494 {ECO:0000313|EMBL:ABX13390.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX13390.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX13390.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX13390.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC {ECO:0000256|HAMAP-Rule:MF_00647}.
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:0000256|HAMAP-
CC Rule:MF_00647};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00647}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00647}.
CC -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000256|HAMAP-
CC Rule:MF_00647}.
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DR EMBL; CP000866; ABX13390.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A4T6; -.
DR STRING; 436308.Nmar_1494; -.
DR EnsemblBacteria; ABX13390; ABX13390; Nmar_1494.
DR KEGG; nmr:Nmar_1494; -.
DR eggNOG; arCOG01223; Archaea.
DR HOGENOM; CLU_035272_5_0_2; -.
DR InParanoid; A9A4T6; -.
DR OrthoDB; 53228at2157; -.
DR PhylomeDB; A9A4T6; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000792; 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 Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00647; PPAT_arch; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR023540; PPAT_arch.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR43793; FAD SYNTHASE; 1.
DR PANTHER; PTHR43793:SF1; FAD SYNTHASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00647};
KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00647};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00647};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00647};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00647}; Reference proteome {ECO:0000313|Proteomes:UP000000792};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00647}.
FT DOMAIN 9..144
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 158 AA; 17371 MW; 0D1603EEF1196CC6 CRC64;
MSQFSLVAMG GTFDIIHRGH ITLLSSAFEI SDKVIIGLTS DEFAKKRGKT LSNNYEKRLA
NLTETIFKEF PKSSFQISKL DNDFGPAVLE PEVQALVVSD ETSSQGDVLN DLRAKKNLSP
VEVITVPMHL AKDGSRISTT RIKNSEIDSE GNLLSVDK
//
