ID   PNKD_BOVIN              Reviewed;         385 AA.
AC   A7YY46;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable hydrolase PNKD;
DE            EC=3.-.-.-;
GN   Name=PNKD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable hydrolase that plays an aggravative role in the
CC       development of cardiac hypertrophy via activation of the NF-kappa-B
CC       signaling pathway. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000305}.
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DR   EMBL; BC151298; AAI51299.1; -; mRNA.
DR   RefSeq; NP_001107642.1; NM_001114170.1.
DR   AlphaFoldDB; A7YY46; -.
DR   SMR; A7YY46; -.
DR   STRING; 9913.ENSBTAP00000005141; -.
DR   PaxDb; A7YY46; -.
DR   PRIDE; A7YY46; -.
DR   GeneID; 616561; -.
DR   KEGG; bta:616561; -.
DR   CTD; 25953; -.
DR   eggNOG; KOG0813; Eukaryota.
DR   HOGENOM; CLU_030571_4_3_1; -.
DR   InParanoid; A7YY46; -.
DR   OrthoDB; 961826at2759; -.
DR   TreeFam; TF105273; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR   CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01374; Glyoxalase_2; 1.
DR   InterPro; IPR035680; Clx_II_MBL.
DR   InterPro; IPR032282; HAGH_C.
DR   InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF16123; HAGH_C; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..385
FT                   /note="Probable hydrolase PNKD"
FT                   /id="PRO_0000311124"
FT   REGION          31..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         291..293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         376..379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  42885 MW;  A906CF6C2265017A CRC64;
     MAAVVAATAL KGRGARNARV LRGILSGATA NKASQNRSRA LQSHSSPECK EEPEPLSPEL
     EYIPRKRGKN PMKAVGLAWY SLYTRTRLGY LFYRQQLRRA RNRYPKGHSR TQPRLFNGVK
     VLPIPVLSDN YSYLIIDTQA RLAVAVDPSD PQAVQASIEK EGVNLVAILC THKHWDHSGG
     NRDLSRRHQD CRVYGSPQDS IPYLTHPLCH QDVVSVGRLQ IRALATPGHT QGHLVYLLDG
     EPYEGPSCLF SGDLLFLSGC GRTFEGTAET MLSSLDTVLG LGDDTLLWPG HEYAEENLGF
     AGVVEPENLA RERKMQWVQR QRMERKSTCP STLGEERSYN PFLRTHCLVL QEALGPSPGP
     TGDDGCSRAQ LLERLRQLKD LHKSK