ID   MDO1_ANAMC              Reviewed;         213 AA.
AC   P83443;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Macrodontain-1;
DE            EC=3.4.22.-;
DE   AltName: Full=Macrodontain I;
OS   Ananas macrodontes (False pineapple) (Pseudananas macrodontes).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=203992 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Fruit;
RX   PubMed=29542000; DOI=10.1007/s12010-018-2725-3;
RA   Errasti M.E., Natalucci C.L., Caffini N.O., Rotelli A.E., Brullo A.,
RA   Maras B., Trejo S.A., Lopez L.M.I.;
RT   "Structural properties of macrodontain I, a cysteine protease from
RT   Pseudananas macrodontes (Morr.) Harms (Bromeliaceae).";
RL   Appl. Biochem. Biotechnol. 186:186-198(2018).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-27, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Fruit;
RX   PubMed=10686143; DOI=10.1006/prep.1999.1165;
RA   Lopez L.M.I., Sequeiros C., Natalucci C.L., Brullo A., Maras B., Barra D.,
RA   Caffini N.O.;
RT   "Purification and characterization of macrodontain I, a cysteine peptidase
RT   from unripe fruits of Pseudananas macrodontes (Morr.) Harms
RT   (Bromeliaceae).";
RL   Protein Expr. Purif. 18:133-140(2000).
RN   [3] {ECO:0000305}
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS
RP   SPECTROMETRY.
RX   PubMed=11517945; DOI=10.1515/bc.2001.108;
RA   Lopez L.M.I., Sequeiros C., Trejo S.A., Pardo M.F., Caffini N.O.,
RA   Natalucci C.L.;
RT   "Comparison of two cysteine endopeptidases from Pseudananas macrodontes
RT   (Morr.) Harms (Bromeliaceae).";
RL   Biol. Chem. 382:875-878(2001).
CC   -!- FUNCTION: Cysteine protease that catalyzes the preferential cleavage:
CC       Ala-|-Xaa > Gln-|-Xaa > Tyr-Xaa >> Leu-|-Xaa > Gly-|-Xaa
CC       (PubMed:10686143, PubMed:11517945). Hydrolyzes the synthetic peptide
CC       substrate Bz-Phe-Val-Arg-pNA (PubMed:11517945).
CC       {ECO:0000269|PubMed:10686143, ECO:0000269|PubMed:11517945}.
CC   -!- ACTIVITY REGULATION: Inhibited by the general cysteine protease
CC       inhibitor E-64 (L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane).
CC       {ECO:0000269|PubMed:10686143, ECO:0000269|PubMed:11517945}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.4 uM for Bz-Phe-Val-Arg-pNA {ECO:0000269|PubMed:11517945};
CC       pH dependence:
CC         Optimum pH is 6.1-8.5. {ECO:0000269|PubMed:10686143,
CC         ECO:0000269|PubMed:11517945};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10686143}.
CC   -!- TISSUE SPECIFICITY: Fruits. {ECO:0000269|PubMed:10686143}.
CC   -!- MASS SPECTROMETRY: Mass=23458.63; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10686143};
CC   -!- MASS SPECTROMETRY: Mass=23459; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11517945};
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   AlphaFoldDB; P83443; -.
DR   SMR; P83443; -.
DR   MEROPS; C01.170; -.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Thiol protease.
FT   CHAIN           1..213
FT                   /note="Macrodontain-1"
FT                   /id="PRO_0000050561"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   DISULFID        23..63
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        57..96
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        153..201
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
SQ   SEQUENCE   213 AA;  23486 MW;  DEB76E632EA77026 CRC64;
     AVPQSIDWRD YGAVNEVKNQ GPCGGCWAFA AIATVEGIYK IRKGNLVYLS EQEVLDCAVS
     YGCKGGWVNR AYDFIISNNG VTTDENYPYR AYQGTCNANY FPNSAYITGY SYVRRNDESH
     MMYAVSNQPI AALIDASGDN FQYYKGGVYS GPCGFSLNHA ITIIGYGRDS YWIVRNSWGS
     SWGQGGYVRI RRDVSHSGGV CGIAMSPLFP TLQ