ID E4ZMB4_LEPMJ Unreviewed; 207 AA.
AC E4ZMB4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|RuleBase:RU004347};
DE EC=2.7.1.25 {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|RuleBase:RU004347};
GN ORFNames=LEMA_P051690.1 {ECO:0000313|EMBL:CBX92463.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|RuleBase:RU004347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000256|RuleBase:RU004347};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}.
CC -!- SIMILARITY: Belongs to the APS kinase family.
CC {ECO:0000256|RuleBase:RU004347}.
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DR EMBL; FP929094; CBX92463.1; -; Genomic_DNA.
DR RefSeq; XP_003835828.1; XM_003835780.1.
DR AlphaFoldDB; E4ZMB4; -.
DR STRING; 985895.E4ZMB4; -.
DR EnsemblFungi; CBX92463; CBX92463; LEMA_P051690.1.
DR GeneID; 13287116; -.
DR eggNOG; KOG0635; Eukaryota.
DR HOGENOM; CLU_046932_1_0_1; -.
DR InParanoid; E4ZMB4; -.
DR OMA; HENTVEE; -.
DR OrthoDB; 22780at2759; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:EnsemblFungi.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; IEA:EnsemblFungi.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004347};
KW Kinase {ECO:0000256|RuleBase:RU004347, ECO:0000313|EMBL:CBX92463.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004347};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ SEQUENCE 207 AA; 23186 MW; E7E4FFACD93E9FC2 CRC64;
MATNITWHPS LSRAERNGFR KQKGFTIWFT GLSASGKSTI ATALEQHLLH LGYAAYRLDG
DNVRFGLNKD LGFTEKDRNE NIRRIAEVAK LFADSSTIAI TSFISPYKKD RATARELHAI
TTGDDEPLAF VEVFVDLPLE VAEARDPKGL YKKAREGKIP EFTGISAPYE APENAEIHIR
SDQKSVEDSV KEITEYLQSK GLLEQLK
//
