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Database: UniProt
Entry: A0A059J5F9_TRIIM
LinkDB: A0A059J5F9_TRIIM
Original site: A0A059J5F9_TRIIM 
ID   A0A059J5F9_TRIIM        Unreviewed;       372 AA.
AC   A0A059J5F9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|RuleBase:RU004347};
DE            EC=2.7.1.25 {ECO:0000256|RuleBase:RU004347};
GN   ORFNames=H109_05063 {ECO:0000313|EMBL:KDB23034.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB23034.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB23034.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB23034.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) 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:KDB23034.1}.
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DR   EMBL; AOKY01000322; KDB23034.1; -; Genomic_DNA.
DR   EMBL; AOKY01000322; KDB23035.1; -; Genomic_DNA.
DR   EMBL; AOKY01000322; KDB23036.1; -; Genomic_DNA.
DR   EMBL; AOKY01000322; KDB23037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059J5F9; -.
DR   HOGENOM; CLU_022950_2_0_1; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000024533; 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:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
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; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU004347};
KW   Kinase {ECO:0000256|RuleBase:RU004347};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004347};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:KDB23034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024533};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
FT   DOMAIN          1..186
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
SQ   SEQUENCE   372 AA;  41369 MW;  2E16C13F4D020446 CRC64;
     MHRAHRELTV RAARARQANV LIHPTVGLTK PGDIDHFTRV RVYEALLPRY PNGMAALGLL
     PLAMRMGGPR EALWHAIIRK NHGCTHFIVG RDHAGPGKNS AGQEMYGPYD AQHLVEKYRD
     ELGIEVVEFQ MLTYLPDSDE YRPHDQVPEG TKTLNISGTE LRKRLRTGAN IPEWFSYPEV
     VKVLRDSNPP RAKQGFTIFL TGYLNSGKAA IARALQVTLN QQGGRPVSLL LGDTVRHELS
     SELGFSREDR DKNIQRIAFV ASELTKAGAA VIAAPIAPYA HSRDAARTTI SSKGSFFLIH
     VATSLEYAEK TDKRGVYARA RRGEIQGFTG VDDPYEAPTN ADLTVDIEKQ SVRSIVHEII
     LMLESQGFLE RS
//
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