ID   GGACB_DANRE             Reviewed;         191 AA.
AC   Q66I06;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Gamma-glutamylaminecyclotransferase B;
DE            Short=GGACT B;
DE            EC=4.3.2.8 {ECO:0000250|UniProtKB:Q9BVM4};
DE   AltName: Full=AIG2-like domain-containing protein 1-B;
DE   AltName: Full=Gamma-glutamylamine cyclotransferase B;
DE   AltName: Full=Gamma-glutamylamine cyclotransferase, tandem duplicate 2;
GN   Name=ggact.2; ORFNames=zgc:92115;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May contribute 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. {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   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BC081599; AAH81599.1; -; mRNA.
DR   RefSeq; NP_001004544.1; NM_001004544.1.
DR   AlphaFoldDB; Q66I06; -.
DR   SMR; Q66I06; -.
DR   STRING; 7955.ENSDARP00000055778; -.
DR   PaxDb; Q66I06; -.
DR   Ensembl; ENSDART00000055779; ENSDARP00000055778; ENSDARG00000038248.
DR   GeneID; 447805; -.
DR   KEGG; dre:447805; -.
DR   CTD; 447805; -.
DR   ZFIN; ZDB-GENE-040912-8; ggact.2.
DR   eggNOG; KOG4450; Eukaryota.
DR   GeneTree; ENSGT00390000010543; -.
DR   HOGENOM; CLU_083466_1_0_1; -.
DR   InParanoid; Q66I06; -.
DR   OMA; YQRTALR; -.
DR   OrthoDB; 1389682at2759; -.
DR   PhylomeDB; Q66I06; -.
DR   TreeFam; TF323258; -.
DR   PRO; PR:Q66I06; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000038248; Expressed in granulocyte and 20 other tissues.
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..191
FT                   /note="Gamma-glutamylaminecyclotransferase B"
FT                   /id="PRO_0000320206"
FT   REGION          155..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        82
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7..10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  22015 MW;  0B22621C8E419E7C CRC64;
     MPLVFVYGTL KKGQPNYFRL IDSSNGQAEF ITCARTVEPY PLVITGECNI PFLLNVPGSG
     QRVYGEIYSV DQKMLEFLDW FEECPDWYQR TLIQLEILKG NGETEVEEAF VYTKTKYEPD
     WLNKPTYDSY DSNGDHGLKY AYEEDMTRST LDQKSADFSQ NSEQEIKKNN SLQILTSTGD
     DHDVNFRGPL Q