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ID C5DCC5_LACTC Unreviewed; 505 AA.
AC C5DCC5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 16-JAN-2019, entry version 66.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03106};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_03106};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_03106};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_03106};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_03106};
GN Name=MET3 {ECO:0000256|HAMAP-Rule:MF_03106};
GN OrderedLocusNames=KLTH0B01914g {ECO:0000313|EMBL:CAR21436.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21436.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR21436.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
CC assimilation, forming adenosine-5'-phosphosulfate (APS) from
CC inorganic sulfate and ATP. Plays an important role in sulfate
CC activation as a component of the biosynthesis pathway of sulfur-
CC containing amino acids. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03106};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000256|HAMAP-
CC Rule:MF_03106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- DOMAIN: The oligomerization domain is distantly related to APS
CC kinases, but it is not functional and does not bind APS. It is
CC required for oligomerization of the enzyme, although the
CC oligomerization state has no effect on the catalytic activity of
CC the enzyme. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_03106}.
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DR EMBL; CU928166; CAR21436.1; -; Genomic_DNA.
DR RefSeq; XP_002551874.1; XM_002551828.1.
DR STRING; 381046.XP_002551874.1; -.
DR EnsemblFungi; CAR21436; CAR21436; KLTH0B01914g.
DR GeneID; 8290702; -.
DR KEGG; lth:KLTH0B01914g; -.
DR HOGENOM; HOG000069044; -.
DR InParanoid; C5DCC5; -.
DR KO; K00958; -.
DR OMA; RMRCYEI; -.
DR OrthoDB; 528280at2759; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002036; Chromosome B.
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; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR CDD; cd00517; ATPS; 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;
DR PRODOM; C5DCC5.
DR SWISS-2DPAGE; C5DCC5.
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03106};
KW Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW Cysteine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03106};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_03106};
KW Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03106}.
FT DOMAIN 3 161 PUA_2. {ECO:0000259|Pfam:PF14306}.
FT DOMAIN 171 385 ATP-sulfurylase. {ECO:0000259|Pfam:
FT PF01747}.
FT NP_BIND 194 197 ATP. {ECO:0000256|HAMAP-Rule:MF_03106}.
FT NP_BIND 288 291 ATP. {ECO:0000256|HAMAP-Rule:MF_03106}.
FT REGION 1 166 N-terminal. {ECO:0000256|HAMAP-Rule:
FT MF_03106}.
FT REGION 167 392 Catalytic. {ECO:0000256|HAMAP-Rule:
FT MF_03106}.
FT REGION 393 505 Required for oligomerization; adenylyl-
FT sulfate kinase-like. {ECO:0000256|HAMAP-
FT Rule:MF_03106}.
FT ACT_SITE 195 195 {ECO:0000256|HAMAP-Rule:MF_03106}.
FT ACT_SITE 196 196 {ECO:0000256|HAMAP-Rule:MF_03106}.
FT ACT_SITE 197 197 {ECO:0000256|HAMAP-Rule:MF_03106}.
FT BINDING 194 194 Sulfate. {ECO:0000256|HAMAP-Rule:
FT MF_03106}.
FT BINDING 196 196 Sulfate. {ECO:0000256|HAMAP-Rule:
FT MF_03106}.
FT BINDING 292 292 Sulfate; via amide nitrogen.
FT {ECO:0000256|HAMAP-Rule:MF_03106}.
FT BINDING 330 330 ATP; via amide nitrogen.
FT {ECO:0000256|HAMAP-Rule:MF_03106}.
FT SITE 200 200 Transition state stabilizer.
FT {ECO:0000256|HAMAP-Rule:MF_03106}.
FT SITE 203 203 Transition state stabilizer.
FT {ECO:0000256|HAMAP-Rule:MF_03106}.
FT SITE 327 327 Induces change in substrate recognition
FT on ATP binding. {ECO:0000256|HAMAP-Rule:
FT MF_03106}.
SQ SEQUENCE 505 AA; 56644 MW; 213DA80C626D9B41 CRC64;
MPAPHGGVLQ DLIARDAQIK DQLLQEAAQA SIKWDLTPRQ ICDLELIQNG GFSPLSGFMN
QKDYDGVVEK SRLSNGLVWT IPINLDVDEA FAKQLKPDAR VVLLQDNEIP VAILTVTDVY
KPDKQNEAKK VFRGDPEHPA VKYLKETAGE YYVGGEIQAI QYPVHYDYPG LRKTPAQLRL
EFDSKQWDRI VAFQTRNPMH RAHRELTVRA AREHNAKVLI HPVVGLTKPG DIDHHTRVRV
YQEIIKRYPN GMAQLSLLPL AMRMGGDREA VWHAIIRKNY GATHFIVGRD HAGPGKNSAG
VDFYGAYDAQ ELVESYKNEL GIEVVPFRMV TYLPEEDRYA PIDQIDLSTT STLNISGTEL
RNRLRSGGPI PEWFSYPEVV KILRESNPPR PKQGFAIVLS SSLKSNKQLS TALLTTFLQF
GGGRHFKVLE HNNDANVLGL VPDFISSGAG LIIPSQYEKW NSVSNAYLVG TSEDADITLD
SDDEAVLHVV QKVVLFLEDH GFFTF
//
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