Q27128 (PAPSS_URECA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase Short name=PAPS synthase Short name=PAPSS Alternative name(s): Sulfurylase kinase Short name=SK Including the following 2 domains: Sulfate adenylyltransferase EC=2.7.7.4 Alternative name(s): ATP-sulfurylase Sulfate adenylate transferase Short name=SAT Adenylyl-sulfate kinase EC=2.7.1.25 Alternative name(s): 3'-phosphoadenosine-5'-phosphosulfate synthase APS kinase Adenosine-5'-phosphosulfate 3'-phosphotransferase Adenylylsulfate 3'-phosphotransferase
Organism	Urechis caupo (Innkeeper worm) (Spoonworm)
Taxonomic identifier	6431 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Annelida › Polychaeta › Echiura › Xenopneusta › Urechidae › Urechis

Protein attributes

Sequence length	610 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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). Ref.1
Catalytic activity	ATP + sulfate = diphosphate + adenylyl sulfate. ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.
Pathway	Sulfur metabolism; sulfate assimilation.
Tissue specificity	In adults expressed in coelomocytes, body wall and gut.
Developmental stage	Expressed in oocytes, embryos and adults.
Sequence similarities	In the N-terminal section; belongs to the APS kinase family. In the C-terminal section; belongs to the sulfate adenylyltransferase family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Nucleotidyltransferase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological_process	sulfate assimilation Inferred from genetic interaction Ref.1. Source: UniProtKB
Molecular_function	ATP binding Non-traceable author statement Ref.1. Source: UniProtKB adenylylsulfate kinase activity Inferred from genetic interaction Ref.1. Source: UniProtKB sulfate adenylyltransferase (ATP) activity Inferred from genetic interaction Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 610	610	Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase		PRO_0000105963
Regions
	Nucleotide binding	44 – 51	8	ATP Potential
	Region	1 – ?205	205	Adenylyl-sulfate kinase
	Region	?206 – 610	405	Sulfate adenylyltransferase
	Motif	506 – 510	5	PP-motif
Sites
	Active site	118	1	Phosphoserine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q27128 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0C7CB61B53AF2F70	FASTA	610	68,475
	10 20 30 40 50 60 MAFLPNGQLA TNVTFQTQHV SRAKRGQVLG QRGGFRGCTV WFTGLSGAGK TTISFALEEY 70 80 90 100 110 120 LVSQGIPTYS LDGDNVRHGL NKNLGFTQED REENIRRISE VAKLFADGGI VCLTSFISPF 130 140 150 160 170 180 KRDRDLARSL HEQAGLPFFE CFVDTPLDVC EQRDVKGLYK KARAGQIKGF TGIDQQYESP 190 200 210 220 230 240 DAPEIQLYAG NKSIDECVQE VVSLLQKNGV VPESAVNIVK ELFVPESGLE HAKAEIVDLP 250 260 270 280 290 300 TMEITKLDTQ WVQVLSEGWA TPLTGFMRER EYLQSQHFGC LLDGGVTNQS IPIVLPVHTA 310 320 330 340 350 360 DKDRLEGSSA FALSYEGKRI AILRTPEFYE HRKEERCSRQ FGTSNAGQPY VKMIMESGDW 370 380 390 400 410 420 LVGGDLEVLE RITWNDGLDE YRLTPNELRA KFRALNADAV FAFQLRNPVH NGHALLMTDT 430 440 450 460 470 480 RRRLTERGYK KPVLLLHPLG GWTKDDDVPL AWRMKQHQAI LDEKVLDPDY TVMAIFPSPM 490 500 510 520 530 540 MYAGPTEVQW HAKARMSTGA NFYIVGRDPA GMPHPETKQD LYNATHGAKV LTMAPGLTQL 550 560 570 580 590 600 EIVPFRVAAY NKTKSAMDFY DPERHDEFMF ISGTKMRGMA RAGETPPNGF MAPSAWKIMV 610 EYYKTKAQQS

References

[1]	"A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities." Rosenthal E., Leustek T. Gene 165:243-248(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L39001 mRNA. Translation: AAB00139.1.
PIR	JC4383.
3D structure databases
ProteinModelPortal	Q27128.
SMR	Q27128. Positions 19-605.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.25. 6574.
UniPathway	UPA00097.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR002891. APS_kinase. IPR025980. ATP-Sase_PUA-like_dom. IPR015947. PUA-like_domain. IPR014729. Rossmann-like_a/b/a_fold. IPR024951. Sulfurylase_cat_dom. IPR002650. Sulphate_adenylyltransferase. [Graphical view]
Pfam	PF01583. APS_kinase. 1 hit. PF01747. ATP-sulfurylase. 1 hit. PF14306. PUA_2. 1 hit. [Graphical view]
SUPFAM	SSF88697. PUA-like. 1 hit.
TIGRFAMs	TIGR00455. apsK. 1 hit. TIGR00339. sopT. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PAPSS_URECA

Accession

Primary (citable) accession number: Q27128

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)