AMZA_METKA
ID AMZA_METKA Reviewed; 175 AA.
AC Q8TXW1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Archaemetzincin {ECO:0000255|HAMAP-Rule:MF_01842};
DE EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_01842, ECO:0000269|PubMed:20597090};
GN Name=amzA {ECO:0000255|HAMAP-Rule:MF_01842}; OrderedLocusNames=MK0548;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [2]
RP MUTAGENESIS OF CYS-163.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION, AND
RP COFACTOR.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=20597090; DOI=10.1002/prot.22777;
RA Waltersperger S., Widmer C., Wang M., Baumann U.;
RT "Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri at
RT 1.5 A resolution.";
RL Proteins 78:2720-2723(2010).
CC -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
CC unknown. Does not show endo- or exopeptidase activity against resorufin
CC labeled casein, p-nitroanilide (pNA), amidomethylcoumarin (AMC) (one to
CC three amino acids in length), and hippuryl-aminoacid substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01842, ECO:0000269|PubMed:20597090}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01842,
CC ECO:0000269|PubMed:20597090};
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:20597090};
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; AE009439; AAM01763.1; -; Genomic_DNA.
DR PDB; 2X7M; X-ray; 1.50 A; A=1-175.
DR PDBsum; 2X7M; -.
DR AlphaFoldDB; Q8TXW1; -.
DR SMR; Q8TXW1; -.
DR STRING; 190192.MK0548; -.
DR EnsemblBacteria; AAM01763; AAM01763; MK0548.
DR KEGG; mka:MK0548; -.
DR HOGENOM; CLU_108521_2_0_2; -.
DR OMA; RSVYDCD; -.
DR EvolutionaryTrace; Q8TXW1; -.
DR Proteomes; UP000001826; 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..175
FT /note="Archaemetzincin"
FT /id="PRO_0000159627"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 125
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 ECO:0000269|PubMed:20597090"
FT BINDING 129
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 ECO:0000269|PubMed:20597090"
FT BINDING 135
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 ECO:0000269|PubMed:20597090"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842,
FT ECO:0000269|PubMed:20597090"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842,
FT ECO:0000269|PubMed:20597090"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842,
FT ECO:0000269|PubMed:20597090"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842,
FT ECO:0000269|PubMed:20597090"
FT MUTAGEN 163
FT /note="C->A: Unstable."
FT /evidence="ECO:0000269|PubMed:22937112"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2X7M"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:2X7M"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2X7M"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2X7M"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2X7M"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2X7M"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:2X7M"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:2X7M"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2X7M"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:2X7M"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2X7M"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:2X7M"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:2X7M"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:2X7M"
SQ SEQUENCE 175 AA; 19827 MW; 95E277E4DE0604BF CRC64;
MKLCLVAFDG RIPMLSSIVD RFEEHVSEYL GEVKVKKKRA KLPEHAYSKV RGQYLARALL
DTLRGMKGEY DRVLGLTSED LYAPGLNFVF GQARCPGREA VVSVARLLDP DPELYLERVV
KELTHELGHT FGLGHCPDRN CVMSFSSSLL EVDRKSPNFC RRCTELLQRN LKRGG
