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Database: UniProt
Entry: A0A397SWY8_9GLOM
LinkDB: A0A397SWY8_9GLOM
Original site: A0A397SWY8_9GLOM 
ID   A0A397SWY8_9GLOM        Unreviewed;       194 AA.
AC   A0A397SWY8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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};
DE   Flags: Fragment;
GN   ORFNames=C1645_726665 {ECO:0000313|EMBL:RIA87264.1};
OS   Glomus cerebriforme.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX   NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA87264.1, ECO:0000313|Proteomes:UP000265703};
RN   [1] {ECO:0000313|EMBL:RIA87264.1, ECO:0000313|Proteomes:UP000265703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA87264.1,
RC   ECO:0000313|Proteomes:UP000265703};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RIA87264.1}.
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DR   EMBL; QKYT01000317; RIA87264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397SWY8; -.
DR   STRING; 658196.A0A397SWY8; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000265703; Unassembled WGS sequence.
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|EMBL:RIA87264.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265703};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
FT   NON_TER         194
FT                   /evidence="ECO:0000313|EMBL:RIA87264.1"
SQ   SEQUENCE   194 AA;  21734 MW;  022D1570AE3EB40F CRC64;
     MSTNITWHEG FVTRSEREEL LKQKGLTIWF TGLSASGKST LASVLEQHLL HLGVASYRLD
     GDNIRFGLNK DLGFGPDDRT ENIRRIAEVA KLFADSTTIA LTSFISPYRA DRDAARKLHE
     DNGIPFVEVF VDAPLEVVEK RDPKGLYKKA KAGEIKEFTG ISSPYEPPTS PELHIQTDKT
     TIEESVKILV NYLK
//
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