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Database: UniProt
Entry: A0A2I1GR55_9GLOM
LinkDB: A0A2I1GR55_9GLOM
Original site: A0A2I1GR55_9GLOM 
ID   A0A2I1GR55_9GLOM        Unreviewed;       203 AA.
AC   A0A2I1GR55;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=RhiirA1_435053 {ECO:0000313|EMBL:PKC61802.1}, RhiirA4_545065
GN   {ECO:0000313|EMBL:PKY49111.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY49111.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY49111.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY49111.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PKC61802.1, ECO:0000313|Proteomes:UP000232688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:PKC61802.1,
RC   ECO:0000313|Proteomes:UP000232688};
RA   Chen E.C.H., Morin E., Baudet D., Noel J., Ndikumana S., Charron P.,
RA   St-Onge C., Giorgi J., Grigoriev I.V., Roux C., Martin F.M., Corradi N.;
RT   "Extensive intraspecific genome diversity in a model arbuscular mycorrhizal
RT   fungus.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PKC61802.1, ECO:0000313|Proteomes:UP000232688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:PKC61802.1,
RC   ECO:0000313|Proteomes:UP000232688};
RA   Corradi N., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2017) 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:PKY49111.1}.
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DR   EMBL; LLXH01000937; PKC61802.1; -; Genomic_DNA.
DR   EMBL; LLXI01000704; PKY49111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1GR55; -.
DR   VEuPathDB; FungiDB:FUN_020701; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1831610; -.
DR   VEuPathDB; FungiDB:RhiirA1_435053; -.
DR   OMA; HENTVEE; -.
DR   OrthoDB; 22780at2759; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000232688; Unassembled WGS sequence.
DR   Proteomes; UP000234323; 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:PKY49111.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ   SEQUENCE   203 AA;  22825 MW;  37B242F16647253F CRC64;
     MMSTNITWHE GQVTRSEREN LLKQKGLTIW FTGLSASGKS TLASVLEQHL LHLGISSYRL
     DGDNIRFGLN KNLGFGPDDR TENIRRIAEV AKLFADSTTI ALTSFISPYK ADRDSARKLH
     EDNGIPFIEV FVDAPLEVVE QRDPKGLYKK AKAGEIKEFT GISSPYEPPT SPELHIQTDK
     TTIEESVKIL VNYLKEKKYI STL
//
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