ID AMPK_PYRFU Reviewed; 346 AA.
AC Q8TZW4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Lysyl aminopeptidase;
DE EC=3.4.11.15;
GN OrderedLocusNames=PF1861;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MASS SPECTROMETRY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15743956; DOI=10.1128/jb.187.6.2077-2083.2005;
RA Story S.V., Shah C., Jenney F.E. Jr., Adams M.W.;
RT "Characterization of a novel zinc-containing, lysine-specific
RT aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 187:2077-2083(2005).
CC -!- FUNCTION: Hydrolyzes di-, tri- and tetrapeptides with a lysine as the
CC N-terminal amino acid and with Gly, Lys, Ala, Phe or Glu in the second
CC position.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferentially, release of N-terminal lysine.; EC=3.4.11.15;
CC Evidence={ECO:0000269|PubMed:15743956};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15743956};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15743956};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 mM for Lys-pNA {ECO:0000269|PubMed:15743956};
CC KM=1.8 mM for Lys-Gly-Gly {ECO:0000269|PubMed:15743956};
CC KM=1.4 mM for Arg-pNA {ECO:0000269|PubMed:15743956};
CC Vmax=2900 umol/min/mg enzyme with Lys-pNA as substrate
CC {ECO:0000269|PubMed:15743956};
CC Vmax=2300 umol/min/mg enzyme with Lys-Gly-Gly as substrate
CC {ECO:0000269|PubMed:15743956};
CC Vmax=1200 umol/min/mg enzyme with Arg-pNA as substrate
CC {ECO:0000269|PubMed:15743956};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:15743956};
CC Temperature dependence:
CC Optimum temperature is 100 degrees Celsius.
CC {ECO:0000269|PubMed:15743956};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15743956}.
CC -!- MASS SPECTROMETRY: Mass=38210; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15743956};
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81985.1; -; Genomic_DNA.
DR RefSeq; WP_011013001.1; NZ_CP023154.1.
DR PDB; 4X8I; X-ray; 2.50 A; A/B/C=1-346.
DR PDBsum; 4X8I; -.
DR AlphaFoldDB; Q8TZW4; -.
DR SMR; Q8TZW4; -.
DR STRING; 186497.PF1861; -.
DR MEROPS; M42.009; -.
DR PaxDb; 186497-PF1861; -.
DR GeneID; 41713681; -.
DR KEGG; pfu:PF1861; -.
DR PATRIC; fig|186497.12.peg.1931; -.
DR eggNOG; arCOG01518; Archaea.
DR HOGENOM; CLU_047249_1_0_2; -.
DR OrthoDB; 30642at2157; -.
DR PhylomeDB; Q8TZW4; -.
DR BRENDA; 3.4.11.15; 5243.
DR SABIO-RK; Q8TZW4; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR NCBIfam; NF040822; lys_aminopep_Arch; 1.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..346
FT /note="Lysyl aminopeptidase"
FT /id="PRO_0000391011"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:4X8I"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4X8I"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:4X8I"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 302..312
FT /evidence="ECO:0007829|PDB:4X8I"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4X8I"
FT HELIX 322..338
FT /evidence="ECO:0007829|PDB:4X8I"
SQ SEQUENCE 346 AA; 38214 MW; 1520E2D6E9A88C28 CRC64;
MVDWELMKKI IESPGVSGYE HLGIRDLVVD ILKDVADEVK IDKLGNVIAH FKGSAPKVMV
AAHMDKIGLM VNHIDKDGYL RVVPIGGVLP ETLIAQKIRF FTEKGERYGV VGVLPPHLRR
EAKDQGGKID WDSIIVDVGA SSREEAEEMG FRIGTIGEFA PNFTRLSEHR FATPYLDDRI
CLYAMIEAAR QLGEHEADIY IVASVQEEIG LRGARVASFA IDPEVGIAMD VTFAKQPNDK
GKIVPELGKG PVMDVGPNIN PKLRQFADEV AKKYEIPLQV EPSPRPTGTD ANVMQINREG
VATAVLSIPI RYMHSQVELA DARDVDNTIK LAKALLEELK PMDFTP
//
