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Archaemetzincin (EC 3.4.-.-)

 AMZA_METKA              Reviewed;         175 AA.
Q8TXW1;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
15-FEB-2017, entry version 67.
RecName: Full=Archaemetzincin {ECO:0000255|HAMAP-Rule:MF_01842};
EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_01842};
Name=amzA {ECO:0000255|HAMAP-Rule:MF_01842}; OrderedLocusNames=MK0548;
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC
100938).
Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
Methanopyrus.
NCBI_TaxID=190192;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
PubMed=11930014; DOI=10.1073/pnas.032671499;
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L.,
Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O.,
Malykh A.G., Koonin E.V., Kozyavkin S.A.;
"The complete genome of hyperthermophile Methanopyrus kandleri AV19
and monophyly of archaeal methanogens.";
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
[2]
MUTAGENESIS OF CYS-163.
STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
PubMed=22937112; DOI=10.1371/journal.pone.0043863;
Graef C., Schacherl M., Waltersperger S., Baumann U.;
"Crystal structures of archaemetzincin reveal a moldable substrate-
binding site.";
PLoS ONE 7:E43863-E43863(2012).
[3]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
AND COFACTOR.
STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
PubMed=20597090; DOI=10.1002/prot.22777;
Waltersperger S., Widmer C., Wang M., Baumann U.;
"Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri
at 1.5 A resolution.";
Proteins 78:2720-2723(2010).
-!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
unknown. Does not show endo- or exopeptidase activity against
resorufin labeled casein, p-nitroanilide (pNA),
amidomethylcoumarin (AMC) (one to three amino acids in length),
and hippuryl-aminoacid substrates. {ECO:0000255|HAMAP-
Rule:MF_01842, ECO:0000269|PubMed:20597090}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090};
Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas
the other seems to have a structural role. {ECO:0000255|HAMAP-
Rule:MF_01842, ECO:0000269|PubMed:20597090};
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01842}.
-!- SIMILARITY: Belongs to the peptidase M54 family.
{ECO:0000255|HAMAP-Rule:MF_01842}.
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EMBL; AE009439; AAM01763.1; -; Genomic_DNA.
PDB; 2X7M; X-ray; 1.50 A; A=1-175.
PDBsum; 2X7M; -.
ProteinModelPortal; Q8TXW1; -.
SMR; Q8TXW1; -.
STRING; 190192.MK0548; -.
MEROPS; M54.001; -.
EnsemblBacteria; AAM01763; AAM01763; MK0548.
KEGG; mka:MK0548; -.
eggNOG; arCOG00458; Archaea.
eggNOG; COG1913; LUCA.
HOGENOM; HOG000223166; -.
KO; K06974; -.
OMA; NNRCVMN; -.
OrthoDB; POG093Z0FT6; -.
EvolutionaryTrace; Q8TXW1; -.
Proteomes; UP000001826; Chromosome.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
CDD; cd11375; Peptidase_M54; 1.
Gene3D; 3.40.390.10; -; 1.
HAMAP; MF_01842; Archaemetzincin; 1.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR012962; Pept_M54_archaemetzincn.
InterPro; IPR012091; Pept_M54_archaemetzncn_arc/bac.
Pfam; PF07998; Peptidase_M54; 1.
PIRSF; PIRSF005785; Zn-prot_arch; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Zinc.
CHAIN 1 175 Archaemetzincin.
/FTId=PRO_0000159627.
ACT_SITE 126 126 Proton acceptor. {ECO:0000305}.
METAL 125 125 Zinc 1; via pros nitrogen; catalytic.
{ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
METAL 129 129 Zinc 1; via pros nitrogen; catalytic.
{ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
METAL 135 135 Zinc 1; via pros nitrogen; catalytic.
{ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
METAL 136 136 Zinc 2. {ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
METAL 141 141 Zinc 2. {ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
METAL 160 160 Zinc 2. {ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
METAL 163 163 Zinc 2. {ECO:0000255|HAMAP-Rule:MF_01842,
ECO:0000269|PubMed:20597090}.
MUTAGEN 163 163 C->A: Unstable.
{ECO:0000269|PubMed:22937112}.
STRAND 2 10 {ECO:0000244|PDB:2X7M}.
HELIX 15 30 {ECO:0000244|PDB:2X7M}.
STRAND 34 39 {ECO:0000244|PDB:2X7M}.
HELIX 44 46 {ECO:0000244|PDB:2X7M}.
TURN 49 52 {ECO:0000244|PDB:2X7M}.
STRAND 53 55 {ECO:0000244|PDB:2X7M}.
HELIX 56 64 {ECO:0000244|PDB:2X7M}.
STRAND 71 79 {ECO:0000244|PDB:2X7M}.
STRAND 89 93 {ECO:0000244|PDB:2X7M}.
STRAND 95 103 {ECO:0000244|PDB:2X7M}.
TURN 105 107 {ECO:0000244|PDB:2X7M}.
HELIX 112 130 {ECO:0000244|PDB:2X7M}.
HELIX 149 154 {ECO:0000244|PDB:2X7M}.
HELIX 161 171 {ECO:0000244|PDB:2X7M}.
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


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