GGACT_BOVIN
ID GGACT_BOVIN Reviewed; 168 AA.
AC Q0VFX9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Gamma-glutamylaminecyclotransferase;
DE Short=GGACT;
DE EC=4.3.2.8 {ECO:0000250|UniProtKB:Q9BVM4};
DE AltName: Full=AIG2-like domain-containing protein 1;
DE AltName: Full=Gamma-glutamylamine cyclotransferase;
GN Name=GGACT; Synonyms=A2LD1;
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=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Contributes to degradation of proteins cross-linked by
CC transglutaminases by degrading the cross-link between a lysine and a
CC glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from
CC L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-
CC alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine
CC and L-gamma-glutamyl-L-alpha-alanine. {ECO:0000250|UniProtKB:Q9BVM4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=epsilon-(gamma-L-glutamyl)-L-lysine = 5-oxo-L-proline + L-
CC lysine; Xref=Rhea:RHEA:16961, ChEBI:CHEBI:32551, ChEBI:CHEBI:58402,
CC ChEBI:CHEBI:133752; EC=4.3.2.8;
CC Evidence={ECO:0000250|UniProtKB:Q9BVM4};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BVM4}.
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC {ECO:0000305}.
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DR EMBL; BC118322; AAI18323.1; -; mRNA.
DR RefSeq; NP_001069039.1; NM_001075571.1.
DR AlphaFoldDB; Q0VFX9; -.
DR SMR; Q0VFX9; -.
DR STRING; 9913.ENSBTAP00000055673; -.
DR PaxDb; Q0VFX9; -.
DR Ensembl; ENSBTAT00000070177; ENSBTAP00000061293; ENSBTAG00000046552.
DR GeneID; 512596; -.
DR KEGG; bta:512596; -.
DR CTD; 87769; -.
DR VEuPathDB; HostDB:ENSBTAG00000046552; -.
DR VGNC; VGNC:29338; GGACT.
DR eggNOG; KOG4450; Eukaryota.
DR GeneTree; ENSGT00390000010543; -.
DR HOGENOM; CLU_083466_1_0_1; -.
DR InParanoid; Q0VFX9; -.
DR OrthoDB; 1389682at2759; -.
DR TreeFam; TF323258; -.
DR BRENDA; 4.3.2.8; 908.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000046552; Expressed in cortex of kidney and 104 other tissues.
DR ExpressionAtlas; Q0VFX9; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0061929; F:gamma-glutamylaminecyclotransferase activity; ISS:UniProtKB.
DR GO; GO:0042219; P:cellular modified amino acid catabolic process; ISS:UniProtKB.
DR CDD; cd06661; GGCT_like; 1.
DR InterPro; IPR009288; AIG2-like_dom.
DR InterPro; IPR039126; GGACT.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR PANTHER; PTHR12510; PTHR12510; 1.
DR Pfam; PF06094; GGACT; 1.
DR SUPFAM; SSF110857; SSF110857; 1.
PE 2: Evidence at transcript level;
KW Lyase; Reference proteome.
FT CHAIN 1..168
FT /note="Gamma-glutamylaminecyclotransferase"
FT /id="PRO_0000320202"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 32..35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 168 AA; 19052 MW; 030326EDF03C30B7 CRC64;
MPGPECKWST TETGAPCGTD DSSGRLAPVF VYGTLKTGQP NHRVLLDGAH GRAAFRGRAH
TLEPYPLVIA GEHNIPRLLN LPGRGHRVFG EVYEVDERML RFLDEFESCP DMYQRTRLHV
ALEGVRGPLE CFVYTTATYP PEWVHLPYLD DYDSQGKHGL RYNPRENR
