ID D7G0D3_ECTSI Unreviewed; 1109 AA.
AC D7G0D3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Similar to 3-phosphoadenosine 5-phosphosulfate synthase 2 isoform 2 {ECO:0000313|EMBL:CBJ26660.1};
GN ORFNames=Esi_0040_0074 {ECO:0000313|EMBL:CBJ26660.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ26660.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ26660.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}.
CC -!- SIMILARITY: Belongs to the PPase family.
CC {ECO:0000256|ARBA:ARBA00006220}.
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DR EMBL; FN648597; CBJ26660.1; -; Genomic_DNA.
DR AlphaFoldDB; D7G0D3; -.
DR STRING; 2880.D7G0D3; -.
DR EnsemblProtists; CBJ26660; CBJ26660; Esi_0040_0074.
DR eggNOG; KOG1626; Eukaryota.
DR eggNOG; KOG4238; Eukaryota.
DR InParanoid; D7G0D3; -.
DR OMA; QGEVDHK; -.
DR OrthoDB; 22780at2759; -.
DR Proteomes; UP000002630; Chromosome LG15.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.80.10; Inorganic pyrophosphatase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; Inorganic pyrophosphatase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 401..586
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 596..808
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 120198 MW; 6A2DBAC236F5C5ED CRC64;
MAVYKYAPVA QDEREKAAAS EAARSSSFSS PSGGGGGIGP LGVPHRRGGG DGDGDDGDSL
ISKRMPYCMA MLVLLAIVYV LARTENAACV CPSLADKPTI PVAELDGGES GAGGWSSADI
PGVPTPPVSP PAAAAQCEPC PSCPVCPAAA PAVRGGGVAE LTCADFDVGK CRKESLEQTT
PHIIECSEAG EGGSQEVCHL PRPQRYAAVG QKGATLWMTG LSGSGKSTIA KALEEELVLR
GGKHVYRLDG DNIRTGLNRD LGFSEADRGE SVRRVGETSC LFSDSGTITI VSLVSPYRDA
RDAVRKRHED QGIPFFEVFL DVPLEEVQRR DPKGLYKQVE EGKLKGFTGV DAPYEPPLNA
ELRLPNMEMT IQECVDALIR VLEAGGILTG GPSDPSGLPM PDGDEIIDLH VAPSEKAALM
AFAETLPKVL ITDIDLNWLQ VIGEGWASPL KGFMREGALL QTIHFASLLV DPANTTGHYN
FNEMDTAFDA LPTHRPPNRV SMSVPIVLPC TGFTKESLES SGMTSAALVT KDGDIVAVIN
DFEIYANRKE EIVSRVFGVI DPGHPYIAHI YSGGDWLIGG EIQLLDRIRY NDGLDKWRLT
ATEVREEFAK KGADVVYAFQ TRNPTHAGHA YLMRTAGEKL RDQGFKNPVL WLSPLGGWTK
PDDVPLDVRV KQHEAVLAEG MLNPDTTVMA IWPSPMIYGG PTEVQFHAKS RRSGGASFFV
VGRDPAGMKG SPEAQAAPDD DLYDAEHGRY VLWMSPGVGS MKMLEFSQVY YDKKTHTMTA
PDPSRQDDFI SISGSKMRQL AAQGAKPCPN DIPSDLLAAN CIPPGFMVQT GWDIVCDYYQ
NVDTKEWVPW SKPVIEPPIA PHTNADGTFG TAPFQLGFTD PTTAKPASPW HDVPLDPGLG
DGVFRFIVEI PMYQTAKMEV MKDVAFNPIM QDESKGKPRY YTYGVPFFNY GLLPQTWEDP
FLKDKEGHGG DNDPLDVMEV GDGPLVMGTI VAVKVLGSLE LIDEGETDHK IIALRVTDPN
AANINNMDDL ERYKPGMTAR LVDWLKMYKT SDGKPPNSLA QDEPTTVDEA LAVIQHTHER
WQSLMAGQAE HDEDFWLGET PETAAGDGW
//
