ID A0A1S3CNL4_CUCME Unreviewed; 207 AA.
AC A0A1S3CNL4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 Name=LOC103502967 {ECO:0000313|RefSeq:XP_008465313.1,
GN ECO:0000313|RefSeq:XP_008465314.1, ECO:0000313|RefSeq:XP_008465315.1,
GN ECO:0000313|RefSeq:XP_008465316.1, ECO:0000313|RefSeq:XP_008465317.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008465317.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008465313.1, ECO:0000313|RefSeq:XP_008465314.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_008465313.1; XM_008467091.2.
DR RefSeq; XP_008465314.1; XM_008467092.2.
DR RefSeq; XP_008465315.1; XM_008467093.2.
DR RefSeq; XP_008465316.1; XM_008467094.2.
DR RefSeq; XP_008465317.1; XM_008467095.2.
DR GeneID; 103502967; -.
DR KEGG; cmo:103502967; -.
DR eggNOG; KOG0635; Eukaryota.
DR OrthoDB; 22780at2759; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
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:0000103; P:sulfate assimilation; IEA:InterPro.
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|RefSeq:XP_008465313.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004347};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ SEQUENCE 207 AA; 23002 MW; 2FFED30E6E5D6B3F CRC64;
MSAVGNGNNI FWHNCPVGKP EREKLLNQKG CVVWITGLSG SGKSTVACSL SRELYALGKI
SYVLDGDNLR HGLNKDLGFK AEDRAENIRR VGEVAKLFAD AGLICIASLI SPYRRDRDFC
RQLLPEANFI EVFMNMPLEL CEARDAKGLY KLAREGKIKG FTGIDDPYEP PLNCEIELRQ
NDGVCPTPCD MAKQIVTFLE EKGFLQA
//
