KAPS_PENCH
ID KAPS_PENCH Reviewed; 211 AA.
AC Q12657;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE Short=APS kinase;
OS Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24791 / PS-75;
RA Foster B.A.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10677210; DOI=10.1021/bi9924157;
RA MacRae I.J., Segel I.H., Fisher A.J.;
RT "Crystal structure of adenosine 5'-phosphosulfate kinase from Penicillium
RT chrysogenum.";
RL Biochemistry 39:1613-1621(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS).
RX PubMed=12427029; DOI=10.1021/bi026556b;
RA Lansdon E.B., Segel I.H., Fisher A.J.;
RT "Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase
RT from Penicillium chrysogenum.";
RL Biochemistry 41:13672-13680(2002).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
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 -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; U39393; AAA81521.1; -; Genomic_DNA.
DR PDB; 1D6J; X-ray; 2.00 A; A/B=1-211.
DR PDB; 1M7G; X-ray; 1.43 A; A/B/C/D=1-211.
DR PDB; 1M7H; X-ray; 2.00 A; A/B/C/D=1-211.
DR PDB; 3CR7; X-ray; 2.50 A; A/B/C/D=23-211.
DR PDBsum; 1D6J; -.
DR PDBsum; 1M7G; -.
DR PDBsum; 1M7H; -.
DR PDBsum; 3CR7; -.
DR AlphaFoldDB; Q12657; -.
DR SMR; Q12657; -.
DR BRENDA; 2.7.1.25; 4606.
DR UniPathway; UPA00140; UER00205.
DR EvolutionaryTrace; Q12657; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis;
KW Kinase; Methionine biosynthesis; Nucleotide-binding; Phosphoprotein;
KW Transferase.
FT CHAIN 1..211
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105932"
FT ACT_SITE 107
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1D6J"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:1M7G"
FT TURN 66..72
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 77..96
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1M7G"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1M7G"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1M7G"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:1M7G"
SQ SEQUENCE 211 AA; 23770 MW; 7DDC4BDA867FE7C2 CRC64;
MSTNITFHAS ALTRSERTEL RNQRGLTIWL TGLSASGKST LAVELEHQLV RDRRVHAYRL
DGDNIRFGLN KDLGFSEADR NENIRRIAEV AKLFADSNSI AITSFISPYR KDRDTARQLH
EVATPGEETG LPFVEVYVDV PVEVAEQRDP KGLYKKAREG VIKEFTGISA PYEAPANPEV
HVKNYELPVQ DAVKQIIDYL DTKGYLPAKK E
