MET3_SCHPO
ID MET3_SCHPO Reviewed; 490 AA.
AC P78937; Q9P6S1; Q9USV5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03106};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_03106};
DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_03106};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_03106};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_03106};
GN Name=sua1; Synonyms=asp1, met3; ORFNames=SPBC27.08c, SPBC28F2.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=caf1-21;
RA Simonics T., Maraz A., Balla E.;
RT "Schizosaccharomyces pombe ATP sulfurylase.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K.,
RA Yanagida M.;
RT "S.pombe chromosome II cosmid 1228 sequence.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
CC assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic
CC sulfate and ATP. Plays an important role in sulfate activation as a
CC component of the biosynthesis pathway of sulfur-containing amino acids.
CC {ECO:0000255|HAMAP-Rule:MF_03106}.
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:0000255|HAMAP-
CC Rule:MF_03106};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000255|HAMAP-
CC Rule:MF_03106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- DOMAIN: The oligomerization domain is distantly related to APS kinases,
CC but it is not functional and does not bind APS. It is required for
CC oligomerization of the enzyme, although the oligomerization state has
CC no effect on the catalytic activity of the enzyme. {ECO:0000255|HAMAP-
CC Rule:MF_03106}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF421374; AAN32720.1; -; Genomic_DNA.
DR EMBL; D83992; BAA12186.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB89007.1; -; Genomic_DNA.
DR PIR; T40044; T40044.
DR RefSeq; NP_595662.2; NM_001021556.3.
DR AlphaFoldDB; P78937; -.
DR SMR; P78937; -.
DR BioGRID; 276950; 15.
DR STRING; 4896.SPBC27.08c.1; -.
DR iPTMnet; P78937; -.
DR MaxQB; P78937; -.
DR PaxDb; P78937; -.
DR PRIDE; P78937; -.
DR EnsemblFungi; SPBC27.08c.1; SPBC27.08c.1:pep; SPBC27.08c.
DR GeneID; 2540422; -.
DR KEGG; spo:SPBC27.08c; -.
DR PomBase; SPBC27.08c; sua1.
DR VEuPathDB; FungiDB:SPBC27.08c; -.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_022950_1_0_1; -.
DR InParanoid; P78937; -.
DR OMA; LQHMIIR; -.
DR PhylomeDB; P78937; -.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:P78937; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IMP:PomBase.
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; IMP:PomBase.
DR GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IMP:PomBase.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IBA:GO_Central.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_03106; Sulf_adenylyltr_euk; 1.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR027535; Sulf_adenylyltr_euk.
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.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..490
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105953"
FT REGION 1..165
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 166..390
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 391..490
FT /note="Required for oligomerization; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 194
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 195
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 193..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 193
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 195
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 287..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 291
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 199
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 202
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 326
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 88
FT /note="A -> P (in Ref. 2; BAA12186)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> I (in Ref. 2; BAA12186)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> D (in Ref. 2; BAA12186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54754 MW; B831C989E9303D85 CRC64;
MTKALLKDLN ARDAPLREQL EQEATSLPKI VLSERQFCDV ELILNGGFSP LDGFMNQKDY
LNVVENLRLS TGEVFPIPIT LDLNESQADS LKAGDRVALL DPRDGQTVIA ILTVEDKYTP
DKANEAEKVF GANDRAHPAV DYLFGRAGNV YVGGKLQAVT PIRHFDFVEY RYSPAQLRSD
FQRNNWNRVV AFQTRNPMHR AHRELTVRAA KQHGARVLIH PVVGMTKPGD IDHFTRVRVY
EAILQRYPKG SAKLSLLPLA MRMAGPREAL WHAIIRKNYG ASHFIIGRDH AGPGKNSQGE
DFYGPYDAQY LVEQYAQEIG ITIVPFQMMT YLPDEDIYKP VDKVEPGTRT LNISGTELRR
RLRVGANIPE WFSYPEVVAI LRQSYPPKYS QGFVLAVPAT SDKLLPSALV SALNEDGRRH
VTLLPRLDAI SVFYAQELQR AGAAVVVSLA DADASVKVPA EWTTVNIKPK DSVSEVTFAV
LSQLSDEGYL
