ID A0A439CWT1_9PEZI Unreviewed; 223 AA.
AC A0A439CWT1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EKO27_g8467 {ECO:0000313|EMBL:RWA06645.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA06645.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA06645.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA06645.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-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:RWA06645.1}.
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DR EMBL; RYZI01000320; RWA06645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439CWT1; -.
DR STRING; 363999.A0A439CWT1; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000286045; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004347};
KW Reference proteome {ECO:0000313|Proteomes:UP000286045};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ SEQUENCE 223 AA; 24771 MW; 95DE9CEE5B19E30E CRC64;
MYNQSHDAPK TMKEARNNIT WHPSLSRAER NDLRKQKGFT LWFTGLSASG KSTVATALEQ
HLLHLGLAAY RLDGDNVRFG LNKDLGFSDK DRTENIRRIG EVAKLFADSS TIALTSFISP
FKADRELARS LHAAQTAGST DEPIAFIEVY VEVPIEVAEQ RDPKGLYKRA RAGEIKEFTG
ISSPYEAPEN PEITIRTAEK SVEECVVDIV AWLEAKGLIP APK
//
