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   16-JUN-2009, entry version 62.
DE   RecName: Full=Adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE            Short=APS kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Penicillium;
OC   Penicillium chrysogenum 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   MEDLINE=20143477; 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
RT   Penicillium chrysogenum.";
RL   Biochemistry 39:1613-1621(2000).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS).
RX   MEDLINE=22314699; 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
RT   kinase from Penicillium chrysogenum.";
RL   Biochemistry 41:13672-13680(2002).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
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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   BRENDA; 2.7.1.25; 285.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA: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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   InterPro; IPR002891; APS_kinase_C.
DR   Pfam; PF01583; APS_kinase; 1.
DR   ProDom; PD002350; APS_kinase; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; ATP-binding;
KW   Cysteine biosynthesis; Kinase; Methionine biosynthesis;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    211       Adenylyl-sulfate kinase.
FT                                /FTId=PRO_0000105932.
FT   NP_BIND      32     39       ATP (Potential).
FT   ACT_SITE    107    107       Phosphoserine intermediate (By
FT                                similarity).
FT   STRAND        4      6
FT   HELIX         7     10
FT   HELIX        14     21
FT   STRAND       26     31
FT   HELIX        38     53
FT   STRAND       57     60
FT   HELIX        62     65
FT   TURN         66     72
FT   HELIX        77     96
FT   STRAND      100    104
FT   HELIX       110    121
FT   STRAND      133    139
FT   HELIX       142    146
FT   HELIX       153    158
FT   STRAND      161    164
FT   TURN        166    168
FT   STRAND      179    183
FT   STRAND      185    187
FT   HELIX       189    202
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
//