ID   SAT_NEOYE               Reviewed;         420 AA.
AC   Q60FC6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Sulfate adenylyltransferase;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
GN   Name=atps {ECO:0000312|EMBL:BAD52446.1};
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD52446.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thallus {ECO:0000312|EMBL:BAD52446.1};
RA   Kanno N., Kogami H.;
RT   "Cloning of cDNA coding for ATP-sulfurylase of Porphyra yezoensis.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAD52446.1}
RP   PROTEIN SEQUENCE OF 2-420, AND ACETYLATION AT ALA-2.
RA   Kanno N., Kogami H.;
RL   Submitted (OCT-2004) to UniProtKB.
RN   [3] {ECO:0000305}
RP   CATALYTIC ACTIVITY.
RA   Kanno N., Sato M., Sato Y.;
RT   "ATP-sulphurylase in marine algae.";
RL   Nippon Suisan Gakkai Shi 53:1047-1050(1987).
RN   [4] {ECO:0000305}
RP   CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RA   Kanno N., Sato M., Sato Y.;
RT   "Properties of ATP-sulphurylase from marine alga Porphyra yezoensis.";
RL   Nippon Suisan Gakkai Shi 54:1635-1639(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|Ref.3,
CC         ECO:0000269|Ref.4};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.4};
CC   -!- ACTIVITY REGULATION: Inhibited by adenosine 5'-phosphosulfate (APS),
CC       but not by 3'phosphoadenosine 5'-phosphosulfate (PAPS). Inhibited by
CC       AMP, ADP, CTP, GTP, ITP, UTP and anions other than those in group IV.
CC       {ECO:0000269|Ref.4}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.2.;
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3.
CC   -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC       {ECO:0000255}.
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DR   EMBL; AB191688; BAD52446.1; -; mRNA.
DR   AlphaFoldDB; Q60FC6; -.
DR   SMR; Q60FC6; -.
DR   UniPathway; UPA00140; UER00204.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   CDD; cd00517; ATPS; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   InterPro; IPR002650; Sulphate_adenylyltransferase.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis;
KW   Direct protein sequencing; Magnesium; Methionine biosynthesis;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..420
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000105956"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   420 AA;  45878 MW;  C5CA346DB026E789 CRC64;
     MANVSPVHGG LSEPVNRVVD SLPSTELLPK IVVNATDYTT LHRIADGTLS PLTGPMTKAD
     YDSVLLKKGI ERDGKLWAWT IPLSLPVTAE EAKALKAGEP AALVSESGDV FGTLTVDAAF
     SWDKPAFLKA VYGTERTDHP GARLWLDDPR TDLVGGSISV LAHDEARPFK DRILYPQSMR
     ALLKEQGYGA SVAFQTRNPL HRAHEYALVY GAEKLLKEVG DSSKVGVFLN PLVGQLKGDD
     VPAATRMETY IKLIDGGFIG EGDMDEELWK SKGQNLREQT RLAGLDMRMF YGGPSEAVMH
     AIYRQNLGIT HFIIGRKHAD APFDDKSAIW GDFDAQEIFE KLEGDLQIKT VNVGFAAYFE
     ELGHVGLCSE NKGKTTVSIS GSKMREMLNS GSMPDSRVMR PATAQVLMDY YAAKNKSATA