PAPSS_URECA
ID PAPSS_URECA Reviewed; 610 AA.
AC Q27128;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase;
DE Short=PAPS synthase;
DE Short=PAPS synthetase {ECO:0000303|PubMed:8522184};
DE Short=PAPSS {ECO:0000303|PubMed:8522184};
DE AltName: Full=Sulfurylase kinase;
DE Short=SK;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4 {ECO:0000305|PubMed:8522184};
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
DE Includes:
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25 {ECO:0000305|PubMed:8522184};
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate synthase;
DE AltName: Full=APS kinase;
DE AltName: Full=Adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenylylsulfate 3'-phosphotransferase;
OS Urechis caupo (Innkeeper worm) (Spoonworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Echiura; Xenopneusta; Urechidae; Urechis.
OX NCBI_TaxID=6431;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8522184; DOI=10.1016/0378-1119(95)00450-k;
RA Rosenthal E., Leustek T.;
RT "A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP
RT sulfurylase and APS kinase activities.";
RL Gene 165:243-248(1995).
CC -!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and adenosine
CC 5'-phosphosulfate (APS) kinase activity, which mediates two steps in
CC the sulfate activation pathway. The first step is the transfer of a
CC sulfate group to ATP to yield APS, and the second step is the transfer
CC of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate
CC (PAPS: activated sulfate donor used by sulfotransferase).
CC {ECO:0000269|PubMed:8522184}.
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:0000305|PubMed:8522184};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18134;
CC Evidence={ECO:0000305|PubMed:8522184};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000305|PubMed:8522184};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153;
CC Evidence={ECO:0000305|PubMed:8522184};
CC -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC {ECO:0000305|PubMed:8522184}.
CC -!- TISSUE SPECIFICITY: In adults expressed in coelomocytes, body wall and
CC gut.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes, embryos and adults.
CC {ECO:0000269|PubMed:8522184}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L39001; AAB00139.1; -; mRNA.
DR PIR; JC4383; JC4383.
DR AlphaFoldDB; Q27128; -.
DR SMR; Q27128; -.
DR BRENDA; 2.7.1.25; 6574.
DR UniPathway; UPA00097; -.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IGI:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IGI:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IGI:UniProtKB.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 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; IPR014729; Rossmann-like_a/b/a_fold.
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; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..610
FT /note="Bifunctional 3'-phosphoadenosine 5'-phosphosulfate
FT synthase"
FT /id="PRO_0000105963"
FT REGION 1..?205
FT /note="Adenylyl-sulfate kinase"
FT REGION ?206..610
FT /note="Sulfate adenylyltransferase"
FT MOTIF 506..510
FT /note="PP-motif"
FT ACT_SITE 118
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 610 AA; 68475 MW; 0C7CB61B53AF2F70 CRC64;
MAFLPNGQLA TNVTFQTQHV SRAKRGQVLG QRGGFRGCTV WFTGLSGAGK TTISFALEEY
LVSQGIPTYS LDGDNVRHGL NKNLGFTQED REENIRRISE VAKLFADGGI VCLTSFISPF
KRDRDLARSL HEQAGLPFFE CFVDTPLDVC EQRDVKGLYK KARAGQIKGF TGIDQQYESP
DAPEIQLYAG NKSIDECVQE VVSLLQKNGV VPESAVNIVK ELFVPESGLE HAKAEIVDLP
TMEITKLDTQ WVQVLSEGWA TPLTGFMRER EYLQSQHFGC LLDGGVTNQS IPIVLPVHTA
DKDRLEGSSA FALSYEGKRI AILRTPEFYE HRKEERCSRQ FGTSNAGQPY VKMIMESGDW
LVGGDLEVLE RITWNDGLDE YRLTPNELRA KFRALNADAV FAFQLRNPVH NGHALLMTDT
RRRLTERGYK KPVLLLHPLG GWTKDDDVPL AWRMKQHQAI LDEKVLDPDY TVMAIFPSPM
MYAGPTEVQW HAKARMSTGA NFYIVGRDPA GMPHPETKQD LYNATHGAKV LTMAPGLTQL
EIVPFRVAAY NKTKSAMDFY DPERHDEFMF ISGTKMRGMA RAGETPPNGF MAPSAWKIMV
EYYKTKAQQS
