APA2_KLULA
ID APA2_KLULA Reviewed; 331 AA.
AC P49348;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 2;
DE Short=Ap4A phosphorylase 2;
DE EC=2.7.7.53;
DE AltName: Full=ADP-sulfurylase;
DE EC=2.7.7.5;
DE AltName: Full=ATP adenylyltransferase;
GN Name=APA2 {ECO:0000303|PubMed:7948033}; OrderedLocusNames=KLLA0C00847g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=7948033; DOI=10.1016/0167-4781(94)90235-6;
RA Mulder W., Scholten I.H.J.M., van Roon H., Grivell L.A.;
RT "Isolation and characterisation of the linked genes APA2 and QCR7, coding
RT for Ap4A phosphorylase II and the 14 kDa subunit VII of the mitochondrial
RT bc1-complex in the yeast Kluyveromyces lactis.";
RL Biochim. Biophys. Acta 1219:719-723(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Ap4A phosphorylase catalyzes the phosphorolytic degradation
CC of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also
CC use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as
CC substrates. Cannot catalyze the reverse reaction. Additionally, this
CC enzyme can also catalyze the phosphorolytic degradation of adenosine
CC 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange
CC reaction between inorganic phosphate and the beta-phosphate of a
CC nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus
CC ATP. {ECO:0000250|UniProtKB:P22108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate +
CC phosphate; Xref=Rhea:RHEA:16577, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58141,
CC ChEBI:CHEBI:456216; EC=2.7.7.53;
CC Evidence={ECO:0000250|UniProtKB:P22108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC phosphate; Xref=Rhea:RHEA:16529, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:43474, ChEBI:CHEBI:58243,
CC ChEBI:CHEBI:456216; EC=2.7.7.5;
CC Evidence={ECO:0000250|UniProtKB:P22108};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P22108};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P22108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22108}. Nucleus
CC {ECO:0000250|UniProtKB:P22108}.
CC -!- SIMILARITY: Belongs to the ATP adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X76027; CAA53616.1; -; Genomic_DNA.
DR EMBL; CR382123; CAH01083.1; -; Genomic_DNA.
DR PIR; S50212; S50212.
DR RefSeq; XP_452232.1; XM_452232.1.
DR AlphaFoldDB; P49348; -.
DR SMR; P49348; -.
DR STRING; 28985.XP_452232.1; -.
DR EnsemblFungi; CAH01083; CAH01083; KLLA0_C00847g.
DR GeneID; 2892615; -.
DR KEGG; kla:KLLA0_C00847g; -.
DR eggNOG; ENOG502QRAQ; Eukaryota.
DR HOGENOM; CLU_049915_1_0_1; -.
DR InParanoid; P49348; -.
DR OMA; LPYANHV; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003877; F:ATP adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004780; F:sulfate adenylyltransferase (ADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR Gene3D; 3.30.428.70; -; 1.
DR InterPro; IPR009163; Ap4A_phos1/2.
DR InterPro; IPR043171; Ap4A_phos1/2-like.
DR InterPro; IPR045759; Ap4A_phos1/2_N.
DR InterPro; IPR019200; ATP_adenylylTrfase_C.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR38420; PTHR38420; 1.
DR Pfam; PF19327; Ap4A_phos_N; 1.
DR Pfam; PF09830; ATP_transf; 1.
DR PIRSF; PIRSF000846; ATP_adenylyltr; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..331
FT /note="Diadenosine 5',5'''-P1,P4-tetraphosphate
FT phosphorylase 2"
FT /id="PRO_0000064612"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 96..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 154..157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 283..285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22108"
SQ SEQUENCE 331 AA; 36991 MW; 8BDB84DDC8597CB7 CRC64;
MFPSNLREIV EATYEKAVAN GHVKFTESSS KKLKDVDAGI SYQVTFAPSL QSKPERLPIA
IDENGAPIPK KDPFAEPEPE LTILDDCAGD YKLLLNKYPV AANHLILVTK KYLLQTAPLS
PKDLLTTYKL LQELDDEDEM LRHLAFYNCG PNSGSSQDHK HLQILPLPYK FVPYQDKLCS
GKEHFIPNAK TEPLQDAKIP FAHYAVPLPE DPEKVDEDLL AMTFVSLLQR TLSMFQDWEG
SNAEKSNDDE ASIPAYNVLM TKEWLCLVPR SKAFAETPSI GFNATGYAGL VLVKWDETLK
VLNENPSAVT KLLLECSFPS TAGAKPTEYH Y
