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AMZA_PYRHO
ID   AMZA_PYRHO              Reviewed;         188 AA.
AC   O59484;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Archaemetzincin {ECO:0000255|HAMAP-Rule:MF_01842};
DE            EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_01842};
GN   Name=amzA {ECO:0000255|HAMAP-Rule:MF_01842}; OrderedLocusNames=PH1820;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
CC       unknown. {ECO:0000255|HAMAP-Rule:MF_01842}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01842};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the
CC       other seems to have a structural role. {ECO:0000255|HAMAP-
CC       Rule:MF_01842};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01842}.
CC   -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01842}.
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DR   EMBL; BA000001; BAA30939.1; -; Genomic_DNA.
DR   PIR; D71193; D71193.
DR   RefSeq; WP_010885879.1; NC_000961.1.
DR   AlphaFoldDB; O59484; -.
DR   SMR; O59484; -.
DR   STRING; 70601.3258256; -.
DR   MEROPS; M54.001; -.
DR   EnsemblBacteria; BAA30939; BAA30939; BAA30939.
DR   GeneID; 1442661; -.
DR   KEGG; pho:PH1820; -.
DR   eggNOG; arCOG00458; Archaea.
DR   OMA; RSVYDCD; -.
DR   OrthoDB; 72411at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd11375; Peptidase_M54; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   HAMAP; MF_01842; Archaemetzincin; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR012962; Pept_M54_archaemetzincn.
DR   InterPro; IPR012091; Pept_M54_archaemetzncn_arc/bac.
DR   PANTHER; PTHR15910; PTHR15910; 1.
DR   Pfam; PF07998; Peptidase_M54; 1.
DR   PIRSF; PIRSF005785; Zn-prot_arch; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..188
FT                   /note="Archaemetzincin"
FT                   /id="PRO_0000159633"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
SQ   SEQUENCE   188 AA;  21416 MW;  CC4A5D58FFD4DC78 CRC64;
     MMGNDSYSSN RGSSRDVLSF LQNFLGGFYA KYGIEVKLVG GLSLSKFYYA FDAERNQFLA
     RHFLPVLSYI KKDFNARAAL GIVNVDIYEP GFNFIFGLAH PGLKVAVVSL YRLYPEFYGN
     PPDRKLLKER ALKEVMHELG HVFGLGHCPN PKCVMHFSNS IIDTDIKSWM YCESCLRKLE
     KNLARSHV
 
 
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