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Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 (PAPS synthase 1) (PAPSS 1) (Sulfurylase kinase 1) (SK 1) (SK1) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)]

 PAPS1_HUMAN             Reviewed;         624 AA.
O43252; O43841; O75332; Q6IAX6; Q96FB1; Q96TF4; Q9P1P9; Q9UE98;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 2.
20-JUN-2018, entry version 187.
RecName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1;
Short=PAPS synthase 1;
Short=PAPSS 1;
AltName: Full=Sulfurylase kinase 1;
Short=SK 1;
Short=SK1;
Includes:
RecName: Full=Sulfate adenylyltransferase;
EC=2.7.7.4 {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121};
AltName: Full=ATP-sulfurylase;
AltName: Full=Sulfate adenylate transferase;
Short=SAT;
Includes:
RecName: Full=Adenylyl-sulfate kinase;
EC=2.7.1.25 {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:17276460, ECO:0000269|PubMed:17540769, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121};
AltName: Full=3'-phosphoadenosine-5'-phosphosulfate synthase;
AltName: Full=APS kinase;
AltName: Full=Adenosine-5'-phosphosulfate 3'-phosphotransferase;
AltName: Full=Adenylylsulfate 3'-phosphotransferase;
Name=PAPSS1; Synonyms=ATPSK1, PAPSS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Tonsil;
PubMed=9576487;
Girard J.-P., Baekkevold E.S., Amalric F.;
"Sulfation in high endothelial venules: cloning and expression of the
human PAPS synthetase.";
FASEB J. 12:603-612(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
PATHWAY, AND VARIANTS PHE-270 AND LEU-587.
TISSUE=Fetal brain;
PubMed=9668121; DOI=10.1074/jbc.273.30.19311;
Venkatachalam K.V., Akita H., Strott C.A.;
"Molecular cloning, expression, and characterization of human
bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its
functional domains.";
J. Biol. Chem. 273:19311-19320(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
TISSUE=Brain;
PubMed=9648242; DOI=10.1271/bbb.62.1037;
Yanagisawa K., Sakakibara Y., Suiko M., Takami Y., Nakayama T.,
Nakajima H., Takayanagi K., Natori Y., Liu M.-C.;
"cDNA cloning, expression, and characterization of the human
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
enzyme.";
Biosci. Biotechnol. Biochem. 62:1037-1040(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-587.
Deyrup A.T.;
"Human ATP sulfurylase/APS kinase.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT LEU-587.
TISSUE=Brain;
PubMed=10679223; DOI=10.1006/bbrc.2000.2123;
Xu Z.-H., Otterness D.M., Freimuth R.R., Carlini E.J., Wood T.C.,
Mitchell S., Moon E., Kim U.-J., Xu J.-P., Siciliano M.J.,
Weinshilboum R.M.;
"Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and
PAPSS2: gene cloning, characterization and chromosomal localization.";
Biochem. Biophys. Res. Commun. 268:437-444(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea {ECO:0000312|EMBL:BAF85463.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
MUTAGENESIS OF HIS-425; ASN-426; GLY-427 AND HIS-428.
PubMed=9915785; DOI=10.1074/jbc.274.5.2601;
Venkatachalam K.V., Fuda H., Koonin E.V., Strott C.A.;
"Site-selected mutagenesis of a conserved nucleotide binding HXGH
motif located in the ATP sulfurylase domain of human bifunctional 3'-
phosphoadenosine 5'-phosphosulfate synthase.";
J. Biol. Chem. 274:2601-2604(1999).
[11]
CRYSTALLIZATION, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PATHWAY.
PubMed=14747722; DOI=10.1107/S0907444903027628;
Harjes S., Scheidig A., Bayer P.;
"Expression, purification and crystallization of human 3'-
phosphoadenosine-5'-phosphosulfate synthetase 1.";
Acta Crystallogr. D 60:350-352(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[14]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH ATP ANALOGS,
SUBUNIT, AND DOMAIN.
PubMed=15755455; DOI=10.1016/j.jmb.2005.01.005;
Harjes S., Bayer P., Scheidig A.J.;
"The crystal structure of human PAPS synthetase 1 reveals asymmetry in
substrate binding.";
J. Mol. Biol. 347:623-635(2005).
[15]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 51-226 IN COMPLEXES WITH ATP
AND 3'-PHOSPHO-5'-ADENYLYL SULFATE ANALOGS, CATALYTIC ACTIVITY,
SUBUNIT, MUTAGENESIS OF ARG-37 AND ARG-40, DOMAIN, AND ENZYME
REGULATION.
PubMed=17540769; DOI=10.1074/jbc.M701713200;
Sekulic N., Konrad M., Lavie A.;
"Structural mechanism for substrate inhibition of the adenosine 5'-
phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-
phosphosulfate synthetase 1 and its ramifications for enzyme
regulation.";
J. Biol. Chem. 282:22112-22121(2007).
[16]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 25-227 IN COMPLEXES WITH
3'-PHOSPHO-5'-ADENYLYL SULFATE AND ADENOSINE-5'-PHOSPHOSULFATE,
CATALYTIC ACTIVITY, AND DOMAIN.
PubMed=17276460; DOI=10.1016/j.jmb.2007.01.025;
Sekulic N., Dietrich K., Paarmann I., Ort S., Konrad M., Lavie A.;
"Elucidation of the active conformation of the APS-kinase domain of
human PAPS synthetase 1.";
J. Mol. Biol. 367:488-500(2007).
-!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS
kinase activity, which mediates two steps in the sulfate
activation pathway. The first step is the transfer of a sulfate
group to ATP to yield adenosine 5'-phosphosulfate (APS), and the
second step is the transfer of a phosphate group from ATP to APS
yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor
used by sulfotransferase). In mammals, PAPS is the sole source of
sulfate; APS appears to be only an intermediate in the sulfate-
activation pathway (PubMed:9576487, PubMed:9668121,
PubMed:9648242, PubMed:14747722). Required for normal biosynthesis
of sulfated L-selectin ligands in endothelial cells
(PubMed:9576487). {ECO:0000269|PubMed:14747722,
ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242,
ECO:0000269|PubMed:9668121}.
-!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
sulfate. {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487,
ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}.
-!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
phosphoadenylyl sulfate. {ECO:0000269|PubMed:14747722,
ECO:0000269|PubMed:17276460, ECO:0000269|PubMed:17540769,
ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242,
ECO:0000269|PubMed:9668121}.
-!- ENZYME REGULATION: Inhibited by chlorate (PubMed:9576487). The
kinase activity is subject to inhibition by the substrate adenylyl
sulfate (PubMed:17540769). {ECO:0000269|PubMed:17540769,
ECO:0000269|PubMed:9576487}.
-!- PATHWAY: Sulfur metabolism; sulfate assimilation.
{ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487,
ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14747722,
ECO:0000269|PubMed:15755455, ECO:0000269|PubMed:17540769}.
-!- TISSUE SPECIFICITY: Expressed in testis, pancreas, kidney, thymus,
prostate, ovary, small intestine, colon, leukocytes and liver.
Also expressed in high endothelial venules (HEV) cells and in
cartilage. {ECO:0000269|PubMed:9576487}.
-!- DOMAIN: The N-terminal first 50 residues are required for
inhibition by the substrate adenylyl sulfate.
{ECO:0000269|PubMed:17540769}.
-!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the sulfate
adenylyltransferase family. {ECO:0000305}.
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EMBL; Y10387; CAA71413.1; -; mRNA.
EMBL; U53447; AAC39894.1; -; Genomic_DNA.
EMBL; AF033026; AAC28429.1; -; mRNA.
EMBL; AF016496; AAD09325.1; -; mRNA.
EMBL; AF105227; AAF40236.1; -; mRNA.
EMBL; AF097721; AAF40235.1; -; Genomic_DNA.
EMBL; AF097710; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097711; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097712; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097713; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097714; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097715; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097716; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097717; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097718; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097719; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AF097720; AAF40235.1; JOINED; Genomic_DNA.
EMBL; AK292774; BAF85463.1; -; mRNA.
EMBL; CR457028; CAG33309.1; -; mRNA.
EMBL; CH471057; EAX06210.1; -; Genomic_DNA.
EMBL; BC011392; AAH11392.1; -; mRNA.
EMBL; BC050627; AAH50627.1; -; mRNA.
CCDS; CCDS3676.1; -.
PIR; JW0087; JW0087.
RefSeq; NP_005434.4; NM_005443.4.
RefSeq; XP_011530702.1; XM_011532400.1.
RefSeq; XP_011530703.1; XM_011532401.1.
UniGene; Hs.368610; -.
PDB; 1X6V; X-ray; 1.75 A; A/B=1-624.
PDB; 1XJQ; X-ray; 2.06 A; A/B=1-624.
PDB; 1XNJ; X-ray; 1.98 A; A/B=1-624.
PDB; 2OFW; X-ray; 2.05 A; A/B/C/D/E/F/G/H=24-225.
PDB; 2OFX; X-ray; 1.90 A; A/B=25-227.
PDB; 2PEY; X-ray; 1.88 A; A/B=51-226.
PDB; 2PEZ; X-ray; 1.40 A; A/B=51-226.
PDB; 2QJF; X-ray; 2.20 A; A/B=220-624.
PDBsum; 1X6V; -.
PDBsum; 1XJQ; -.
PDBsum; 1XNJ; -.
PDBsum; 2OFW; -.
PDBsum; 2OFX; -.
PDBsum; 2PEY; -.
PDBsum; 2PEZ; -.
PDBsum; 2QJF; -.
ProteinModelPortal; O43252; -.
SMR; O43252; -.
BioGrid; 114522; 48.
IntAct; O43252; 13.
STRING; 9606.ENSP00000265174; -.
DrugBank; DB03708; Adenosine-5'-Phosphosulfate.
DrugBank; DB04077; Glycerol.
iPTMnet; O43252; -.
PhosphoSitePlus; O43252; -.
BioMuta; PAPSS1; -.
EPD; O43252; -.
PaxDb; O43252; -.
PeptideAtlas; O43252; -.
PRIDE; O43252; -.
ProteomicsDB; 48837; -.
DNASU; 9061; -.
Ensembl; ENST00000265174; ENSP00000265174; ENSG00000138801.
GeneID; 9061; -.
KEGG; hsa:9061; -.
UCSC; uc003hyk.4; human.
CTD; 9061; -.
DisGeNET; 9061; -.
EuPathDB; HostDB:ENSG00000138801.8; -.
GeneCards; PAPSS1; -.
HGNC; HGNC:8603; PAPSS1.
HPA; HPA049781; -.
MIM; 603262; gene.
neXtProt; NX_O43252; -.
OpenTargets; ENSG00000138801; -.
PharmGKB; PA384; -.
eggNOG; KOG0635; Eukaryota.
eggNOG; KOG4238; Eukaryota.
eggNOG; COG0529; LUCA.
eggNOG; COG2046; LUCA.
GeneTree; ENSGT00390000009613; -.
HOVERGEN; HBG053503; -.
KO; K13811; -.
OMA; CKEHPYI; -.
OrthoDB; EOG091G07ZR; -.
PhylomeDB; O43252; -.
TreeFam; TF313143; -.
BioCyc; MetaCyc:HS06566-MONOMER; -.
BRENDA; 2.7.1.25; 2681.
BRENDA; 2.7.7.4; 2681.
Reactome; R-HSA-174362; Transport and synthesis of PAPS.
Reactome; R-HSA-2408550; Metabolism of ingested H2SeO4 and H2SeO3 into H2Se.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
SABIO-RK; O43252; -.
UniPathway; UPA00097; -.
ChiTaRS; PAPSS1; human.
EvolutionaryTrace; O43252; -.
GeneWiki; PAPSS1; -.
GenomeRNAi; 9061; -.
PRO; PR:O43252; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138801; -.
CleanEx; HS_PAPSS1; -.
Genevisible; O43252; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IDA:UniProtKB.
GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; IDA:UniProtKB.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0000103; P:sulfate assimilation; IDA:UniProtKB.
CDD; cd02027; APSK; 1.
CDD; cd00517; ATPS; 1.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_00065; Adenylyl_sulf_kinase; 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; IPR024951; Sulfurylase_cat_dom.
InterPro; IPR002650; Sulphate_adenylyltransferase.
Pfam; PF01747; ATP-sulfurylase; 1.
Pfam; PF14306; PUA_2; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00455; apsK; 1.
TIGRFAMs; TIGR00339; sopT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Kinase;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Polymorphism; Reference proteome; Transferase.
CHAIN 1 624 Bifunctional 3'-phosphoadenosine 5'-
phosphosulfate synthase 1.
/FTId=PRO_0000105959.
NP_BIND 62 67 ATP 1. {ECO:0000244|PDB:1X6V,
ECO:0000244|PDB:1XJQ,
ECO:0000244|PDB:1XNJ,
ECO:0000244|PDB:2OFX,
ECO:0000244|PDB:2PEY,
ECO:0000244|PDB:2PEZ,
ECO:0000269|PubMed:15755455,
ECO:0000269|PubMed:17276460,
ECO:0000269|PubMed:17540769}.
NP_BIND 419 422 ATP 2. {ECO:0000244|PDB:1XJQ,
ECO:0000244|PDB:1XNJ,
ECO:0000244|PDB:2QJF,
ECO:0000269|PubMed:15755455}.
NP_BIND 521 525 ATP 2. {ECO:0000244|PDB:1XJQ,
ECO:0000244|PDB:1XNJ,
ECO:0000244|PDB:2QJF,
ECO:0000269|PubMed:15755455}.
REGION 1 225 Adenylyl-sulfate kinase.
{ECO:0000305|PubMed:15755455,
ECO:0000305|PubMed:17276460,
ECO:0000305|PubMed:17540769}.
REGION 89 92 Adenylyl sulfate binding.
{ECO:0000244|PDB:2OFX,
ECO:0000305|PubMed:17276460}.
REGION 106 109 Adenylyl sulfate binding.
{ECO:0000244|PDB:2OFX,
ECO:0000244|PDB:2PEZ,
ECO:0000305|PubMed:17276460,
ECO:0000305|PubMed:17540769}.
REGION 132 133 Adenylyl sulfate binding.
{ECO:0000244|PDB:2OFX,
ECO:0000244|PDB:2PEZ,
ECO:0000305|PubMed:17276460,
ECO:0000305|PubMed:17540769}.
REGION 184 185 Adenylyl sulfate binding.
{ECO:0000244|PDB:2OFX,
ECO:0000244|PDB:2PEZ,
ECO:0000305|PubMed:17276460,
ECO:0000305|PubMed:17540769}.
REGION 234 624 Sulfate adenylyltransferase.
{ECO:0000305|PubMed:15755455}.
BINDING 101 101 Adenylyl sulfate. {ECO:0000244|PDB:2OFX,
ECO:0000305|PubMed:17276460}.
BINDING 171 171 Adenylyl sulfate. {ECO:0000244|PDB:2OFX,
ECO:0000305|PubMed:17276460}.
BINDING 207 207 ATP 1; via carbonyl oxygen.
{ECO:0000244|PDB:1X6V,
ECO:0000244|PDB:1XJQ,
ECO:0000244|PDB:1XNJ,
ECO:0000244|PDB:2OFW,
ECO:0000244|PDB:2OFX,
ECO:0000244|PDB:2PEY,
ECO:0000244|PDB:2PEZ,
ECO:0000269|PubMed:15755455,
ECO:0000269|PubMed:17276460,
ECO:0000269|PubMed:17540769}.
BINDING 212 212 ATP 1. {ECO:0000244|PDB:2OFX,
ECO:0000269|PubMed:17276460}.
BINDING 563 563 ATP 2; via amide nitrogen and carbonyl
oxygen. {ECO:0000244|PDB:1XJQ,
ECO:0000244|PDB:1XNJ,
ECO:0000244|PDB:2QJF,
ECO:0000269|PubMed:15755455}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 12 12 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q60967}.
VARIANT 270 270 L -> F (in dbSNP:rs1127008).
{ECO:0000269|PubMed:9668121}.
/FTId=VAR_014065.
VARIANT 587 587 S -> L (in dbSNP:rs1127014).
{ECO:0000269|PubMed:10679223,
ECO:0000269|PubMed:9668121,
ECO:0000269|Ref.4}.
/FTId=VAR_014064.
MUTAGEN 37 37 R->A: Abolishes inhibition by the
substrate adenylyl sulfate.
{ECO:0000269|PubMed:17540769}.
MUTAGEN 40 40 R->A: Abolishes inhibition by the
substrate adenylyl sulfate.
{ECO:0000269|PubMed:17540769}.
MUTAGEN 425 425 H->A: Loss of activity.
{ECO:0000269|PubMed:9915785}.
MUTAGEN 426 426 N->K: Increased activity.
{ECO:0000269|PubMed:9915785}.
MUTAGEN 427 428 GH->AA: Loss of activity.
MUTAGEN 427 427 G->A: 30% decrease in activity.
{ECO:0000269|PubMed:9915785}.
MUTAGEN 428 428 H->A: Loss of activity.
{ECO:0000269|PubMed:9915785}.
CONFLICT 456 456 G -> A (in Ref. 1; CAA71413).
{ECO:0000305}.
CONFLICT 456 456 Missing (in Ref. 2; AAC39894).
{ECO:0000305}.
CONFLICT 519 520 IV -> MC (in Ref. 4; AAD09325).
{ECO:0000305}.
HELIX 37 43 {ECO:0000244|PDB:1X6V}.
STRAND 44 49 {ECO:0000244|PDB:1X6V}.
STRAND 53 58 {ECO:0000244|PDB:2PEZ}.
HELIX 65 78 {ECO:0000244|PDB:2PEZ}.
STRAND 83 87 {ECO:0000244|PDB:2PEZ}.
HELIX 88 91 {ECO:0000244|PDB:2PEZ}.
TURN 92 98 {ECO:0000244|PDB:2PEZ}.
HELIX 103 122 {ECO:0000244|PDB:2PEZ}.
STRAND 126 130 {ECO:0000244|PDB:2PEZ}.
HELIX 136 148 {ECO:0000244|PDB:2PEZ}.
STRAND 153 159 {ECO:0000244|PDB:2PEZ}.
HELIX 162 168 {ECO:0000244|PDB:2PEZ}.
HELIX 173 178 {ECO:0000244|PDB:2PEZ}.
STRAND 181 184 {ECO:0000244|PDB:2OFX}.
TURN 186 188 {ECO:0000244|PDB:2PEZ}.
STRAND 199 203 {ECO:0000244|PDB:2PEZ}.
TURN 204 206 {ECO:0000244|PDB:2PEZ}.
HELIX 209 222 {ECO:0000244|PDB:2PEZ}.
HELIX 241 243 {ECO:0000244|PDB:1X6V}.
HELIX 244 252 {ECO:0000244|PDB:1X6V}.
STRAND 256 258 {ECO:0000244|PDB:1X6V}.
HELIX 261 271 {ECO:0000244|PDB:1X6V}.
TURN 272 277 {ECO:0000244|PDB:1X6V}.
HELIX 284 293 {ECO:0000244|PDB:1X6V}.
STRAND 294 296 {ECO:0000244|PDB:1X6V}.
STRAND 310 312 {ECO:0000244|PDB:1X6V}.
HELIX 314 320 {ECO:0000244|PDB:1X6V}.
STRAND 324 330 {ECO:0000244|PDB:1X6V}.
STRAND 333 345 {ECO:0000244|PDB:1X6V}.
HELIX 348 356 {ECO:0000244|PDB:1X6V}.
HELIX 364 371 {ECO:0000244|PDB:1X6V}.
STRAND 374 383 {ECO:0000244|PDB:1X6V}.
HELIX 394 396 {ECO:0000244|PDB:1X6V}.
HELIX 400 409 {ECO:0000244|PDB:1X6V}.
STRAND 413 422 {ECO:0000244|PDB:1X6V}.
HELIX 426 442 {ECO:0000244|PDB:1X6V}.
STRAND 445 454 {ECO:0000244|PDB:1X6V}.
HELIX 465 477 {ECO:0000244|PDB:1X6V}.
HELIX 483 485 {ECO:0000244|PDB:1X6V}.
STRAND 486 488 {ECO:0000244|PDB:1X6V}.
HELIX 499 512 {ECO:0000244|PDB:1X6V}.
STRAND 516 520 {ECO:0000244|PDB:1X6V}.
TURN 530 532 {ECO:0000244|PDB:1X6V}.
STRAND 534 537 {ECO:0000244|PDB:1X6V}.
HELIX 541 548 {ECO:0000244|PDB:1X6V}.
STRAND 556 559 {ECO:0000244|PDB:1X6V}.
STRAND 563 566 {ECO:0000244|PDB:1X6V}.
TURN 567 570 {ECO:0000244|PDB:1X6V}.
STRAND 571 574 {ECO:0000244|PDB:1X6V}.
HELIX 580 582 {ECO:0000244|PDB:1X6V}.
HELIX 588 596 {ECO:0000244|PDB:1X6V}.
HELIX 608 621 {ECO:0000244|PDB:1X6V}.
SEQUENCE 624 AA; 70833 MW; A3DC9B943E68CDD6 CRC64;
MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL
SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF
ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG
EIKGFTGIDS EYEKPEAPEL VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP
ENKLHLAKTD AETLPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG
VINLSVPIVL TATHEDKERL DGCTAFALMY EGRRVAILRN PEFFEHRKEE RCARQWGTTC
KNHPYIKMVM EQGDWLIGGD LQVLDRVYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL
RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGV
LNPETTVVAI FPSPMMYAGP TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPS
HGAKVLTMAP GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK
PPEGFMAPKA WTVLTEYYKS LEKA


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