MET3_CANAL
ID MET3_CANAL Reviewed; 527 AA.
AC Q9Y872; A0A1D8PFS8; Q5AKV2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=MET3 {ECO:0000255|HAMAP-Rule:MF_03106};
GN OrderedLocusNames=CAALFM_C113870WA; ORFNames=CaO19.12492, CaO19.5025;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=124;
RX PubMed=10564518; DOI=10.1046/j.1365-2958.1999.01641.x;
RA Care R.S., Trevethick J., Binley K.M., Sudbery P.E.;
RT "The MET3 promoter: a new tool for Candida albicans molecular genetics.";
RL Mol. Microbiol. 34:792-798(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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DR EMBL; AF164103; AAD45374.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW26989.1; -; Genomic_DNA.
DR RefSeq; XP_722228.1; XM_717135.1.
DR AlphaFoldDB; Q9Y872; -.
DR SMR; Q9Y872; -.
DR BioGRID; 1219192; 2.
DR STRING; 237561.Q9Y872; -.
DR PRIDE; Q9Y872; -.
DR GeneID; 3636132; -.
DR KEGG; cal:CAALFM_C113870WA; -.
DR CGD; CAL0000178072; MET3.
DR VEuPathDB; FungiDB:C1_13870W_A; -.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_022950_1_0_1; -.
DR InParanoid; Q9Y872; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 528280at2759; -.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:Q9Y872; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IBA:GO_Central.
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:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IBA:GO_Central.
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; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..527
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105952"
FT REGION 1..176
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 177..406
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 407..527
FT /note="Required for oligomerization; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 208
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 209
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 206..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 206
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 208
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 302..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 306
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 212
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 341
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT CONFLICT 139
FT /note="E -> K (in Ref. 1; AAD45374)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> P (in Ref. 1; AAD45374)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="H -> D (in Ref. 1; AAD45374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 58859 MW; 05D9050CDE97F9BA CRC64;
MPIPTPHGGK LRDLVIRDAP LKQQLLQEAK TLPALTLTAR QLCDLELILN GGFSPLTGFL
NQEDYNSVVN DLRLSSVKNE SNGKGLLWPI PITLDVDETT SKKHSVGDRI VLIDLRDETP
LAILTIESIY KPDKKLEAEK VFRGDSEHPA NKYLLETAGD YYIGGELQGI NYPKHYDYVD
ARKTPTELRQ EFEKLGWAQE NIVAFQTRNP MHRAHRELTI RAAQDIGDKA HILIHPVVGL
TKPGDIDHHT RVKVYKQILT KFPDGLATLS LLPLAMRMGG DREALWHALI RTNYGVDHFI
VGRDHAGPGK NSQGVDFYGP YDAQELLAKY DDELNIKIVP FRMVTYLPDE DRYAPIDTID
VKKVRTANIS GTELRNKLKT GDEIPSWFSY PEVVKILRET NPPRSKQGFA ILIDNSHKLG
DYLSFALQST LNQFSGERRI TKLNAHQAND SFIVGELVKA GSGVIVPTTN PTPIVNVVGN
GNSLVVNQKN NNNQASGNAD GEFNLSNDDL VAVVDEIVNY LKDQGFY
