HAGHL_CHICK
ID HAGHL_CHICK Reviewed; 282 AA.
AC Q5ZLY2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Hydroxyacylglutathione hydrolase-like protein;
DE EC=3.1.2.-;
GN Name=HAGHL; ORFNames=RCJMB04_21j14, RCJMB04_4h5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Hydrolase acting on ester bonds. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AJ719602; CAG31261.1; -; mRNA.
DR EMBL; AJ851726; CAH65360.1; -; mRNA.
DR RefSeq; NP_001025808.1; NM_001030637.1.
DR AlphaFoldDB; Q5ZLY2; -.
DR SMR; Q5ZLY2; -.
DR STRING; 9031.ENSGALP00000008654; -.
DR PaxDb; Q5ZLY2; -.
DR Ensembl; ENSGALT00000008668; ENSGALP00000008654; ENSGALG00000021040.
DR GeneID; 416536; -.
DR KEGG; gga:416536; -.
DR CTD; 84264; -.
DR VEuPathDB; HostDB:geneid_416536; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000161924; -.
DR HOGENOM; CLU_030571_4_0_1; -.
DR InParanoid; Q5ZLY2; -.
DR OMA; CKERARF; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q5ZLY2; -.
DR TreeFam; TF105273; -.
DR PRO; PR:Q5ZLY2; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000021040; Expressed in lung and 13 other tissues.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IBA:GO_Central.
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; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..282
FT /note="Hydroxyacylglutathione hydrolase-like protein"
FT /id="PRO_0000313603"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 32228 MW; C1595401229CFD2E CRC64;
MKVKVISVLE DNYMYLVIEE STRDAVAVDA AVPKRLLEIV RKEDVVLRAV LITHHHWDHA
RGNEELVRLC PGLRVYGADE RIGALTHRVA PDEELTFGAI RVRCLFTPCH TKGHMCYFMW
EDGSLDAPAL FSGDTLFVGG CGQFLEGTAE QMYTNLTQVL GDLPKETKVF CGHECTVRNL
KFALKVEPEN EAVKKKLAWA RQRDDEDLPT VPSTLQEEFL YNPFLRVTEE AVQKFTGRKE
PVEVLRALRT EKDNFKKPKE RPHPQAMLAF DWGLFAPFLE KK