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Database: UniProt
Entry: A0A2I4HWE5_JUGRE
LinkDB: A0A2I4HWE5_JUGRE
Original site: A0A2I4HWE5_JUGRE 
ID   A0A2I4HWE5_JUGRE        Unreviewed;       276 AA.
AC   A0A2I4HWE5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=LOC109022093 {ECO:0000313|RefSeq:XP_018860442.1};
GN   ORFNames=F2P56_013806 {ECO:0000313|EMBL:KAF5463654.1};
OS   Juglans regia (English walnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Juglandaceae; Juglans.
OX   NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018860442.1};
RN   [1] {ECO:0000313|EMBL:KAF5463654.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5463654.1};
RA   Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA   Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA   Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA   Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA   Wegrzyn J.L., Langley C.H., Neale D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF5463654.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5463654.1};
RA   Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA   Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA   Salzberg S.L., Neale D.B.;
RT   "Walnut 2.0.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_018860442.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaves {ECO:0000313|RefSeq:XP_018860442.1};
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   EMBL; LIHL02000007; KAF5463654.1; -; Genomic_DNA.
DR   RefSeq; XP_018860442.1; XM_019004897.2.
DR   STRING; 51240.A0A2I4HWE5; -.
DR   EnsemblPlants; Jr07_00650_p1; cds.Jr07_00650_p1; Jr07_00650.
DR   GeneID; 109022093; -.
DR   Gramene; Jr07_00650_p1; cds.Jr07_00650_p1; Jr07_00650.
DR   KEGG; jre:109022093; -.
DR   OrthoDB; 22780at2759; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000235220; Chromosome 7.
DR   Proteomes; UP000619265; Unassembled WGS sequence.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:SF63; ADENYLYL-SULFATE KINASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 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_018860442.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ   SEQUENCE   276 AA;  30304 MW;  A7038F1892D800FE CRC64;
     MALKLGSASL WETNAMGLNH KADKRLAALH GVDVRSSFLK PVKATSGYSN NAASLINDCV
     VISGKNFHQM ATVGKSTNIV WHKCPVEKFD RQELLMQKGC VIWITGLSGS GKSTLACTLN
     RGLHSRGKLT YILDGDNVRH GLNNDLSFKA EDRAENIRRI GEVAKLFADA GIICIASLIS
     PFKKDRDDCR ALLPEGDFIE VFLDVPLEVC EARDPKGLYK LARSGKIKGF TGIDDPYEPP
     VNCEIVLQQK GEDCISPCEM AETVISYLEE RGYLQA
//
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