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Thermostable carboxypeptidase 1 (EC 3.4.17.19) (Carboxypeptidase Pfu) (PfuCP)

 CBP1_PYRFU              Reviewed;         499 AA.
Q8U3L0;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
07-JUN-2017, entry version 85.
RecName: Full=Thermostable carboxypeptidase 1;
EC=3.4.17.19;
AltName: Full=Carboxypeptidase Pfu;
Short=PfuCP;
OrderedLocusNames=PF0456;
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=186497;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=10430560;
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
DiRuggiero J., Robb F.T.;
"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
P. horikoshii inferred from complete genomic sequences.";
Genetics 152:1299-1305(1999).
[2]
PROTEIN SEQUENCE OF 1-30; 41-72 AND 480-495, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ENZYME
REGULATION.
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=10595552; DOI=10.1110/ps.8.11.2474;
Cheng T.C., Ramakrishnan V., Chan S.I.;
"Purification and characterization of a cobalt-activated
carboxypeptidase from the hyperthermophilic archaeon Pyrococcus
furiosus.";
Protein Sci. 8:2474-2486(1999).
[3]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
LEAD IONS, SUBUNIT, AND COFACTOR.
PubMed=11839307; DOI=10.1016/S0969-2126(02)00698-6;
Arndt J.W., Hao B., Ramakrishnan V., Cheng T., Chan S.I., Chan M.K.;
"Crystal structure of a novel carboxypeptidase from the
hyperthermophilic archaeon Pyrococcus furiosus.";
Structure 10:215-224(2002).
-!- FUNCTION: Broad specificity carboxypetidase that releases amino
acids sequentially from the C-terminus, including neutral,
aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.
{ECO:0000269|PubMed:10595552}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
specificity, except for -Pro. {ECO:0000269|PubMed:10595552}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:10595552,
ECO:0000269|PubMed:11839307};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:10595552,
ECO:0000269|PubMed:11839307};
Note=Binds 1 cobalt ion per subunit. Can also utilize Mn(2+) (in
vitro). Is not active with zinc ions.
{ECO:0000269|PubMed:10595552, ECO:0000269|PubMed:11839307};
-!- ENZYME REGULATION: EDTA and DTT reversibly abolish
carboxypeptidase activity. {ECO:0000269|PubMed:10595552}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.2-6.6. {ECO:0000269|PubMed:10595552};
Temperature dependence:
Optimum temperature is 90-100 degrees Celsius.
{ECO:0000269|PubMed:10595552};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10595552,
ECO:0000269|PubMed:11839307}.
-!- SIMILARITY: Belongs to the peptidase M32 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE009950; AAL80580.1; -; Genomic_DNA.
RefSeq; WP_011011573.1; NC_003413.1.
PDB; 1K9X; X-ray; 2.30 A; A/B/C/D=1-499.
PDB; 1KA2; X-ray; 2.20 A; A=1-499.
PDB; 1KA4; X-ray; 3.00 A; A=1-499.
PDBsum; 1K9X; -.
PDBsum; 1KA2; -.
PDBsum; 1KA4; -.
ProteinModelPortal; Q8U3L0; -.
SMR; Q8U3L0; -.
STRING; 186497.PF0456; -.
MEROPS; M32.002; -.
PRIDE; Q8U3L0; -.
EnsemblBacteria; AAL80580; AAL80580; PF0456.
GeneID; 1468297; -.
KEGG; pfu:PF0456; -.
PATRIC; fig|186497.12.peg.480; -.
eggNOG; arCOG04247; Archaea.
eggNOG; COG2317; LUCA.
HOGENOM; HOG000040803; -.
KO; K01299; -.
OMA; EFGHALY; -.
OrthoDB; POG093Z01FT; -.
BRENDA; 3.4.17.B5; 5243.
EvolutionaryTrace; Q8U3L0; -.
Proteomes; UP000001013; Chromosome.
GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd06460; M32_Taq; 1.
InterPro; IPR001333; Peptidase_M32_Taq.
Pfam; PF02074; Peptidase_M32; 1.
PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
PRINTS; PR00998; CRBOXYPTASET.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Cobalt; Complete proteome;
Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
Protease; Reference proteome.
CHAIN 1 499 Thermostable carboxypeptidase 1.
/FTId=PRO_0000428834.
ACT_SITE 270 270 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P42663}.
METAL 269 269 Cobalt; catalytic.
{ECO:0000269|PubMed:11839307}.
METAL 273 273 Cobalt; catalytic.
{ECO:0000269|PubMed:11839307}.
METAL 299 299 Cobalt. {ECO:0000269|PubMed:11839307}.
HELIX 8 36 {ECO:0000244|PDB:1KA2}.
HELIX 40 42 {ECO:0000244|PDB:1KA2}.
HELIX 43 61 {ECO:0000244|PDB:1KA2}.
HELIX 64 74 {ECO:0000244|PDB:1KA2}.
HELIX 81 99 {ECO:0000244|PDB:1KA2}.
HELIX 102 124 {ECO:0000244|PDB:1KA2}.
HELIX 128 130 {ECO:0000244|PDB:1KA2}.
HELIX 132 149 {ECO:0000244|PDB:1KA2}.
HELIX 155 163 {ECO:0000244|PDB:1KA2}.
HELIX 169 192 {ECO:0000244|PDB:1KA2}.
HELIX 201 203 {ECO:0000244|PDB:1KA2}.
HELIX 209 223 {ECO:0000244|PDB:1KA2}.
TURN 228 230 {ECO:0000244|PDB:1KA2}.
STRAND 231 235 {ECO:0000244|PDB:1KA2}.
STRAND 241 245 {ECO:0000244|PDB:1KA2}.
STRAND 248 253 {ECO:0000244|PDB:1KA2}.
HELIX 261 278 {ECO:0000244|PDB:1KA2}.
HELIX 282 284 {ECO:0000244|PDB:1KA2}.
HELIX 295 306 {ECO:0000244|PDB:1KA2}.
TURN 307 311 {ECO:0000244|PDB:1KA2}.
HELIX 313 326 {ECO:0000244|PDB:1KA2}.
HELIX 328 332 {ECO:0000244|PDB:1KA2}.
HELIX 335 342 {ECO:0000244|PDB:1KA2}.
HELIX 351 353 {ECO:0000244|PDB:1KA2}.
TURN 356 358 {ECO:0000244|PDB:1KA2}.
HELIX 359 375 {ECO:0000244|PDB:1KA2}.
HELIX 380 382 {ECO:0000244|PDB:1KA2}.
HELIX 383 395 {ECO:0000244|PDB:1KA2}.
HELIX 402 404 {ECO:0000244|PDB:1KA2}.
TURN 405 407 {ECO:0000244|PDB:1KA2}.
HELIX 411 414 {ECO:0000244|PDB:1KA2}.
HELIX 421 440 {ECO:0000244|PDB:1KA2}.
HELIX 444 450 {ECO:0000244|PDB:1KA2}.
HELIX 454 463 {ECO:0000244|PDB:1KA2}.
HELIX 465 467 {ECO:0000244|PDB:1KA2}.
HELIX 473 481 {ECO:0000244|PDB:1KA2}.
HELIX 488 498 {ECO:0000244|PDB:1KA2}.
SEQUENCE 499 AA; 59043 MW; 627A8347CD899BC0 CRC64;
MEEVFQNETI KQILAKYRRI WAIGHAQSVL GWDLEVNMPK EGILERSVAQ GELSVLSHEL
LLHPEFVNLV EKAKGLENLN EYERGIVRVL DRSIRIARAF PPEFIREVSE TTSLATKAWE
EAKAKDDFSK FEPWLDKIIS LAKRAAEYLG YEEEPYDALL DLYEEGLRTR DVEKMFEVLE
KKLKPLLDKI LEEGKVPREH PLEKEKYERE WMERVNLWIL QKFGFPLGTR ARLDVSAHPF
TTEFGIRDVR ITTRYEGYDF RRTILSTVHE FGHALYELQQ DERFMFTPIA GGVSLGIHES
QSRFWENIIG RSKEFVELIY PVLKENLPFM SNYTPEDVYL YFNIVRPDFI RTEADVVTYN
FHILLRFKLE RLMVSEEIKA KDLPEMWNDE MERLLGIRPR KYSEGILQDI HWAHGSIGYF
PTYTIGTLLS AQLYYHIKKD IPDFEEKVAK AEFDPIKAWL REKIHRWGSI YPPKELLKKA
IGEDMDAEYF VRWVKEKYL


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