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Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT)

 A0A084FVT8_9PEZI        Unreviewed;       574 AA.
A0A084FVT8;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
22-NOV-2017, entry version 23.
RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03106};
EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_03106};
AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_03106};
AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_03106};
Short=SAT {ECO:0000256|HAMAP-Rule:MF_03106};
Name=MET3 {ECO:0000256|HAMAP-Rule:MF_03106};
ORFNames=SAPIO_CDS9861 {ECO:0000313|EMBL:KEZ39200.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ39200.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ39200.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ39200.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
assimilation, forming adenosine-5'-phosphosulfate (APS) from
inorganic sulfate and ATP. Plays an important role in sulfate
activation as a component of the biosynthesis pathway of sulfur-
containing amino acids. {ECO:0000256|HAMAP-Rule:MF_03106}.
-!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
sulfate. {ECO:0000256|HAMAP-Rule:MF_03106}.
-!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_03106}.
-!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000256|HAMAP-
Rule:MF_03106}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03106}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ39200.1}.
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EMBL; JOWA01000154; KEZ39200.1; -; Genomic_DNA.
RefSeq; XP_016638999.1; XM_016791155.1.
EnsemblFungi; KEZ39200; KEZ39200; SAPIO_CDS9861.
GeneID; 27728933; -.
UniPathway; UPA00140; UER00204.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
CDD; cd02027; APSK; 1.
CDD; cd00517; ATPS; 1.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_03106; Sulf_adenylyltr_euk; 1.
InterPro; IPR002891; APS_kinase.
InterPro; IPR025980; ATP-Sase_PUA-like_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR027535; Sulf_adenylyltr_euk.
InterPro; IPR024951; Sulfurylase_cat_dom.
InterPro; IPR002650; Sulphate_adenylyltransferase.
Pfam; PF01747; ATP-sulfurylase; 1.
Pfam; PF14306; PUA_2; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00455; apsK; 1.
TIGRFAMs; TIGR00339; sopT; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03106};
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cysteine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106};
Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03106};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_03106,
ECO:0000313|EMBL:KEZ39200.1};
Reference proteome {ECO:0000313|Proteomes:UP000028545};
Transferase {ECO:0000256|HAMAP-Rule:MF_03106,
ECO:0000313|EMBL:KEZ39200.1}.
DOMAIN 4 165 PUA_2. {ECO:0000259|Pfam:PF14306}.
DOMAIN 175 388 ATP-sulfurylase.
{ECO:0000259|Pfam:PF01747}.
NP_BIND 197 201 ATP. {ECO:0000256|HAMAP-Rule:MF_03106}.
NP_BIND 292 296 ATP. {ECO:0000256|HAMAP-Rule:MF_03106}.
REGION 1 170 N-terminal. {ECO:0000256|HAMAP-
Rule:MF_03106}.
ACT_SITE 199 199 {ECO:0000256|HAMAP-Rule:MF_03106}.
ACT_SITE 200 200 {ECO:0000256|HAMAP-Rule:MF_03106}.
ACT_SITE 201 201 {ECO:0000256|HAMAP-Rule:MF_03106}.
BINDING 207 207 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03106}.
BINDING 334 334 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03106}.
BINDING 357 357 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03106}.
BINDING 358 358 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03106}.
SITE 204 204 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_03106}.
SITE 207 207 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_03106}.
SITE 331 331 Induces change in substrate recognition
on ATP binding. {ECO:0000256|HAMAP-
Rule:MF_03106}.
SEQUENCE 574 AA; 64657 MW; 826D8F4FD2166F7F CRC64;
MPLTPHGGVL KDLFARDLPR KEELAAEADT LPALTLSERH LCDLELILNG GFSPLEGFLN
EKDYNGVVKN LRLESGVLFS MPITLDVDRA TVDELGIKTG ARITLRDFRD ERNLAILTVE
DVYRPDRNLE AREVFGSEDD THPGVHYVLN VAKEFYVGGK LEALHRLDHY DFLDLRYTPA
ELRAHFDKLG WQRVVAFQTR NPMHRAHREL TVRAARSQQA NVLIHPVVGL TKPGDIDHFT
RVRVYKAILP RYPNGMASLA LLPLAMRMGG PREAIWHAII RKNHGATHFI VGRDHAGPGK
NKQGVDHYGP YDAQEAVKKY QDELGIKMVE FQEMIYLPDR DEYMPRNEVP EGVRTTNISG
TELRYRLRTG KEIPEWFSYP EVVKVLREQN PLPSAKGFTV FLTGYQNSGK DQVARALQAT
LMQGGGRPVS MLLGETVRHE LSAELGFSRE DRKTNIARIA FVASELTKAG AAVIAAPIAP
YEDARVQARE LIEKSGPFFL IHVATPLEYC EKTDRRGIYK KARAGEIKGF TGVDDPYEVP
PAADLVVDRE KQTVRSIVHE IILLLESRGL LDRL


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