MET3_PENCH
ID MET3_PENCH Reviewed; 572 AA.
AC Q12650;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03106};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_03106};
DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_03106};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_03106};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_03106};
GN Name=met3 {ECO:0000255|HAMAP-Rule:MF_03106}; Synonyms=APS;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 24791 / PS-75;
RX PubMed=8051058; DOI=10.1016/s0021-9258(17)32088-4;
RA Foster B.A., Thomas S.M., Mahr J.A., Renosto F., Patel H.C., Segel I.H.;
RT "Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum.
RT Identification of a likely allosteric domain.";
RL J. Biol. Chem. 269:19777-19786(1994).
RN [2]
RP PROTEIN SEQUENCE OF 487-517.
RX PubMed=2545683; DOI=10.1016/s0021-9258(18)80132-6;
RA Martin R.L., Daley L.A., Lovric Z., Wailes L.M., Renosto F., Segel I.H.;
RT "The 'regulatory' sulfhydryl group of Penicillium chrysogenum ATP
RT sulfurylase. Cooperative ligand binding after SH modification; chemical and
RT thermodynamic properties.";
RL J. Biol. Chem. 264:11768-11775(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP ALLOSTERIC INHIBITOR.
RX PubMed=11389593; DOI=10.1021/bi010367w;
RA MacRae I.J., Segel I.H., Fisher A.J.;
RT "Crystal structure of ATP sulfurylase from Penicillium chrysogenum:
RT insights into the allosteric regulation of sulfate assimilation.";
RL Biochemistry 40:6795-6804(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR.
RX PubMed=12426581; DOI=10.1038/nsb868;
RA MacRae I.J., Segel I.H., Fisher A.J.;
RT "Allosteric inhibition via R-state destabilization in ATP sulfurylase from
RT Penicillium chrysogenum.";
RL Nat. Struct. Biol. 9:945-949(2002).
CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
CC assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic
CC sulfate and ATP. Plays an important role in sulfate activation as a
CC component of the biosynthesis pathway of sulfur-containing amino acids.
CC {ECO:0000255|HAMAP-Rule:MF_03106}.
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:0000255|HAMAP-
CC Rule:MF_03106};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by 3'-phosphoadenosine
CC 5'-phosphosulfate (PAPS). {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000255|HAMAP-
CC Rule:MF_03106, ECO:0000269|PubMed:11389593,
CC ECO:0000269|PubMed:12426581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- DOMAIN: The adenylyl-sulfate kinase (APS kinase) is non-functional. It
CC is involved in allosteric regulation by PAPS. PAPS binding induces a
CC large rotational rearrangement of domains lowering the substrate
CC affinity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC family. {ECO:0000255|HAMAP-Rule:MF_03106}.
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DR EMBL; U07353; AAA20839.1; -; mRNA.
DR PIR; A59274; A53651.
DR PDB; 1I2D; X-ray; 2.81 A; A/B/C=1-572.
DR PDB; 1M8P; X-ray; 2.60 A; A/B/C=1-572.
DR PDBsum; 1I2D; -.
DR PDBsum; 1M8P; -.
DR AlphaFoldDB; Q12650; -.
DR SMR; Q12650; -.
DR PRIDE; Q12650; -.
DR BRENDA; 2.7.7.4; 4606.
DR SABIO-RK; Q12650; -.
DR UniPathway; UPA00140; UER00204.
DR EvolutionaryTrace; Q12650; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; IEA:InterPro.
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_03106; Sulf_adenylyltr_euk; 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; IPR027535; Sulf_adenylyltr_euk.
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 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..572
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105951"
FT REGION 1..169
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000305|PubMed:11389593"
FT REGION 170..393
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000305|PubMed:11389593"
FT REGION 394..572
FT /note="Allosteric regulation domain; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000305|PubMed:11389593"
FT ACT_SITE 198
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 199
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 200
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 197..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:11389593"
FT BINDING 197
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:11389593"
FT BINDING 199
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:11389593"
FT BINDING 291..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:11389593"
FT BINDING 295
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:11389593"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:11389593"
FT BINDING 433..436
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:12426581"
FT BINDING 450
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:12426581"
FT BINDING 476..477
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:12426581"
FT BINDING 514
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000269|PubMed:12426581"
FT SITE 203
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106,
FT ECO:0000305|PubMed:11389593"
FT SITE 330
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1I2D"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1I2D"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1I2D"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1I2D"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 408..422
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 432..438
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 447..466
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 480..491
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 505..511
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 516..521
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:1M8P"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:1M8P"
FT HELIX 552..565
FT /evidence="ECO:0007829|PDB:1M8P"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:1M8P"
SQ SEQUENCE 572 AA; 63917 MW; 4C921D76FD1988E1 CRC64;
MANAPHGGVL KDLLARDAPR QAELAAEAES LPAVTLTERQ LCDLELIMNG GFSPLEGFMN
QADYDRVCED NRLADGNVFS MPITLDASQE VIDEKKLQAA SRITLRDFRD DRNLAILTID
DIYRPDKTKE AKLVFGGDPE HPAIVYLNNT VKEFYIGGKI EAVNKLNHYD YVALRYTPAE
LRVHFDKLGW SRVVAFQTRN PMHRAHRELT VRAARSRQAN VLIHPVVGLT KPGDIDHFTR
VRAYQALLPR YPNGMAVLGL LGLAMRMGGP REAIWHAIIR KNHGATHFIV GRDHAGPGSN
SKGEDFYGPY DAQHAVEKYK DELGIEVVEF QMVTYLPDTD EYRPVDQVPA GVKTLNISGT
ELRRRLRSAH IPEWFSYPEV VKILRESNPP RATQGFTIFL TGYMNSGKDA IARALQVTLN
QQGGRSVSLL LGDTVRHELS SELGFTREDR HTNIQRIAFV ATELTRAGAA VIAAPIAPYE
ESRKFARDAV SQAGSFFLVH VATPLEHCEQ SDKRGIYAAA RRGEIKGFTG VDDPYETPEK
ADLVVDFSKQ SVRSIVHEII LVLESQGFLE RQ
