ID Q1CZQ0_MYXXD Unreviewed; 501 AA.
AC Q1CZQ0;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN OrderedLocusNames=MXAN_5988 {ECO:0000313|EMBL:ABF86647.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86647.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF86647.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC -!- SIMILARITY: Belongs to the peptidase M32 family.
CC {ECO:0000256|PIRNR:PIRNR006615}.
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DR EMBL; CP000113; ABF86647.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1CZQ0; -.
DR STRING; 246197.MXAN_5988; -.
DR EnsemblBacteria; ABF86647; ABF86647; MXAN_5988.
DR KEGG; mxa:MXAN_5988; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_1_7; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd06460; M32_Taq; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:ABF86647.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:ABF86647.1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 501 AA; 56379 MW; B81790E1B140224D CRC64;
MNPGMDTWLL TRMQELRDLQ GLIGLATWDM ETYLPSKAGP ARSHQLSTLQ GLHHERLVDP
RLGEALAQAA SQADLSDDAR AMVTVLTRER EREVRVPAPL VRALAGAISD AIQAWREARQ
ARRFTVFQPA LQRLLSLRRE QADAYGHDGE RYDALLEGHE PGMRVARLTP VLSALREHLI
PMVGKLTAVS RPVAPFLMGR HYDKDTQWAF TLRLLKDIGF DLEAGRQDLS IHPFTGGTHP
LDVRLTTHVD TATPFPSIFS TIHEAGHGLY EQGFAPELYR TPLAAAPSMG LHESQSRLWE
NMVGRGLPFW RHYFPVLRAA FPEALSGTDL ETFHAAVNAV GPSLIRIESD EVTYNLHIAL
RYELELLLVR DELPVEDLPA AWNARMEKYL GITPPDDTQG VLQDIHWAWG ELGYFPTYSL
GNLYAASLYR AAKRDLPELE AHLGRGELLP LRDWLRTHVH QHGFRHSAEE RVKQVTGQGL
TDTDFLAYLK EKYGALYGVS L
//
