(data stored in ACNUC8465 zone)

SWISSPROT: C5DCC5_LACTC

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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