ID   BROM1_ANACO             Reviewed;         351 AA.
AC   O23791;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Fruit bromelain;
DE            EC=3.4.22.33;
DE   AltName: Allergen=Ana c 2;
DE   Flags: Precursor;
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. N67-10; TISSUE=Fruit;
RA   Muta E., Aramaki H., Takata Y., Kono A., Okamoto Y., Ota S.;
RT   "Cloning and sequencing of fruit bromelain.";
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds. Bz-Phe-Val-Arg-|-NHMec is a good synthetic substrate, but
CC         there is no action on Z-Arg-Arg-|-NHMec (cf. stem bromelain).;
CC         EC=3.4.22.33;
CC   -!- ALLERGEN: Causes an allergic reaction in human.
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   EMBL; D14059; BAA21849.1; -; mRNA.
DR   PIR; T10503; T10503.
DR   AlphaFoldDB; O23791; -.
DR   SMR; O23791; -.
DR   Allergome; 3076; Ana c 2.0101.
DR   Allergome; 694; Ana c 2.
DR   MEROPS; C01.028; -.
DR   BRENDA; 3.4.22.33; 333.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
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   Allergen; Disulfide bond; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..121
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000045809"
FT   CHAIN           122..351
FT                   /note="Fruit bromelain"
FT                   /id="PRO_0000045810"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000250"
FT   DISULFID        144..184
FT                   /evidence="ECO:0000250"
FT   DISULFID        178..217
FT                   /evidence="ECO:0000250"
FT   DISULFID        273..325
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  39055 MW;  33781C55144242B0 CRC64;
     MASKVQLVFL FLFLCAMWAS PSAASRDEPN DPMMKRFEEW MAEYGRVYKD DDEKMRRFQI
     FKNNVKHIET FNSRNENSYT LGINQFTDMT KSEFVAQYTG VSLPLNIERE PVVSFDDVNI
     SAVPQSIDWR DYGAVNEVKN QNPCGSCWSF AAIATVEGIY KIKTGYLVSL SEQEVLDCAV
     SYGCKGGWVN KAYDFIISNN GVTTEENYPY LAYQGTCNAN SFPNSAYITG YSYVRRNDER
     SMMYAVSNQP IAALIDASEN FQYYNGGVFS GPCGTSLNHA ITIIGYGQDS SGTKYWIVRN
     SWGSSWGEGG YVRMARGVSS SSGVCGIAMA PLFPTLQSGA NAEVIKMVSE T