Reviewed, UniProtKB/Swiss-Prot Q12657 (KAPS_PENCH)

Names and origin

Protein names	Recommended name:     Adenylyl-sulfate kinase     EC=2.7.1.25 Alternative name(s):     Adenosine-5'-phosphosulfate kinase       Short name=APS kinase     ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
Organism	Penicillium chrysogenum (Penicillium notatum)
Taxonomic identifier	5076 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium › Penicillium chrysogenum complex

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the synthesis of activated sulfate.
Catalytic activity	ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the APS kinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Methionine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylylsulfate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Adenylyl-sulfate kinase

PRO_0000105932

Regions

Nucleotide binding

32 – 39

8

ATP Potential

Sites

Active site

107

1

Phosphoserine intermediate By similarity

Secondary structure

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211

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

7 – 10

4

Helix

14 – 21

8

Beta strand

26 – 31

6

Helix

38 – 53

16

Beta strand

57 – 60

4

Helix

62 – 65

4

Turn

66 – 72

7

Helix

77 – 96

20

Beta strand

100 – 104

5

Helix

110 – 121

12

Beta strand

133 – 139

7

Helix

142 – 146

5

Helix

153 – 158

6

Beta strand

161 – 164

4

Turn

166 – 168

3

Beta strand

179 – 183

5

Beta strand

185 – 187

3

Helix

189 – 202

14

Sequences

	Sequence		Length	Mass (Da)
	Q12657-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7DDC4BDA867FE7C2	FASTA	211	23,770
	10 20 30 40 50 60 MSTNITFHAS ALTRSERTEL RNQRGLTIWL TGLSASGKST LAVELEHQLV RDRRVHAYRL 70 80 90 100 110 120 DGDNIRFGLN KDLGFSEADR NENIRRIAEV AKLFADSNSI AITSFISPYR KDRDTARQLH 130 140 150 160 170 180 EVATPGEETG LPFVEVYVDV PVEVAEQRDP KGLYKKAREG VIKEFTGISA PYEAPANPEV 190 200 210 HVKNYELPVQ DAVKQIIDYL DTKGYLPAKK E

References

[1]	Foster B.A. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24791 / PS-75.
[2]	"Crystal structure of adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum." MacRae I.J., Segel I.H., Fisher A.J. Biochemistry 39:1613-1621(2000) [PubMed: 10677210] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[3]	"Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum." Lansdon E.B., Segel I.H., Fisher A.J. Biochemistry 41:13672-13680(2002) [PubMed: 12427029] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U39393 Genomic DNA. Translation: AAA81521.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D6J	X-ray	2.00	A/B	1-211	[»]
1M7G	X-ray	1.43	A/B/C/D	1-211	[»]
1M7H	X-ray	2.00	A/B/C/D	1-211	[»]
3CR7	X-ray	2.50	A/B/C/D	23-211	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.7.1.25. 285.

Family and domain databases

InterPro

IPR002891. APS_kinase_C.
[Graphical view]

Pfam

PF01583. APS_kinase. 1 hit.
[Graphical view]

ProDom

PD002350. APS_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00455. apsK. 1 hit.

ProtoNet

Search...

Entry information

Entry name

KAPS_PENCH

Accession

Primary (citable) accession number: Q12657

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)