AMZA_ARCFU
ID AMZA_ARCFU Reviewed; 160 AA.
AC O29917;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=AF_0330;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEXES WITH ZINC, COFACTOR,
RP ACTIVE SITE, AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=22937112; DOI=10.1371/journal.pone.0043863;
RA Graef C., Schacherl M., Waltersperger S., Baumann U.;
RT "Crystal structures of archaemetzincin reveal a moldable substrate-binding
RT site.";
RL PLoS ONE 7:E43863-E43863(2012).
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 ECO:0000269|PubMed:22937112};
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, ECO:0000269|PubMed:22937112};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01842,
CC ECO:0000269|PubMed:22937112}.
CC -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000255|HAMAP-
CC Rule:MF_01842}.
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DR EMBL; AE000782; AAB90906.1; -; Genomic_DNA.
DR PIR; B69291; B69291.
DR RefSeq; WP_010877837.1; NC_000917.1.
DR PDB; 3ZVS; X-ray; 1.40 A; A/B/C=1-160.
DR PDB; 4A3W; X-ray; 2.16 A; A=1-160.
DR PDB; 4AXQ; X-ray; 1.45 A; A=1-160.
DR PDBsum; 3ZVS; -.
DR PDBsum; 4A3W; -.
DR PDBsum; 4AXQ; -.
DR AlphaFoldDB; O29917; -.
DR SMR; O29917; -.
DR STRING; 224325.AF_0330; -.
DR EnsemblBacteria; AAB90906; AAB90906; AF_0330.
DR GeneID; 24793869; -.
DR KEGG; afu:AF_0330; -.
DR eggNOG; arCOG00458; Archaea.
DR HOGENOM; CLU_108521_2_0_2; -.
DR OMA; KDRGQYH; -.
DR OrthoDB; 72411at2157; -.
DR PhylomeDB; O29917; -.
DR EvolutionaryTrace; O29917; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..160
FT /note="Archaemetzincin"
FT /id="PRO_0000159623"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:22937112"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:3ZVS"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3ZVS"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:3ZVS"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:3ZVS"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:3ZVS"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3ZVS"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 104..122
FT /evidence="ECO:0007829|PDB:3ZVS"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:3ZVS"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:3ZVS"
SQ SEQUENCE 160 AA; 17888 MW; 6D85AD127388970D CRC64;
MKIYIQPLSV NSHTVEVLAN SLPKIFNAEV FVLPASDVSL KCYNASRRQY NSTCILRMLP
PIKVTLGVTG KDIYAKGMNF VFGEAELGGA RAVLSVFRLT TADSELYRER VVKEAVHEIG
HVLGLKHCSN NCVMRFSNSV QDVDRKPVSF CRECASKIRY
