MBLAC2
entrez
153364
canonical
uniprot
Q68D91
canonical
ensembl
ENSG00000176055
resolver
ensp
ENSP00000314776
resolver
genesymbol
MBLAC2
resolver
hgnc
HGNC:33711
resolver
uniprot
B3KY36
resolver
uniprot
D6RJI1
resolver
uniprot
Q8IY16
resolver
uniprot
Q8N8D8
resolver
uniprot_entry
B3KY36_HUMAN
resolver
uniprot_entry
MBLC2_HUMAN
resolver
uniprot_sec
D6RJI1
resolver
uniprot_sec
Q8IY16
resolver
uniprot_sec
Q8N8D8
resolver
activity_regulation
ACTIVITY REGULATION: Beta-lactamase activity is inhibited by sulbactam. {ECO:0000269|PubMed:31434986}.
uniprot
proteins
amino_acid_sequence
MSALEWYAHKSLGDGIFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLQDREAKEDAARRPLLAVATHVHFDHSGGLYQFDRVAVHHAEAEALARGDNFETVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGHFNTFGAERLFRLASNYISKAGICHKVSTFAMRSLASLALRVTNSRTSP
uniprot
proteins
ec_number
3.1.2.2
uniprot
proteins
ec_number
3.5.2.6
uniprot
proteins
function
FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:33219126). Has an acyl-CoA thioesterase activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:33219126). Displays a substrate preference for fatty acyl-CoAs with chain-lengths C12-C18 (PubMed:33219126). Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (PubMed:31434986). Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (PubMed:31434986). {ECO:0000269|PubMed:31434986, ECO:0000269|PubMed:33219126}.
uniprot
proteins
mass_dalton
31372
uniprot
proteins
mutagenesis
MUTAGEN 87; /note="D->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:33219126"; MUTAGEN 88; /note="H->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:33219126"; MUTAGEN 89; /note="S->A: No effect on enzyme activity."; /evidence="ECO:0000269|PubMed:33219126"; MUTAGEN 93; /note="Y->A: No effect on enzyme activity."; /evidence="ECO:0000269|PubMed:33219126"; MUTAGEN 176; /note="C->A: No effect on ZDHH20-catalyzed palmitoylation."; /evidence="ECO:0000269|PubMed:33219126"; MUTAGEN 212; /note="C->A: No effect on ZDHH20-catalyzed palmitoylation."; /evidence="ECO:0000269|PubMed:33219126"; MUTAGEN 254; /note="C->A: Loss of ZDHH20-catalyzed palmitoylation. Shows only a slight reduction in the Vmax and a small increase in the Km towards palmitoyl-CoA in comparison with wild-type."; /evidence="ECO:0000269|PubMed:33219126
uniprot
proteins
post_translational_modification
PTM: Palmitoylated on Cys-254 by ZDHHC20. {ECO:0000269|PubMed:33219126}.
uniprot
proteins
protein_family
Glyoxalase II family
uniprot
proteins
protein_family
Metallo-beta-lactamase superfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
31434986
uniprot
proteins
pubmed
33219126
uniprot
proteins
sequence_length
279
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33219126}; Lipid-anchor {ECO:0000269|PubMed:33219126}. Cell membrane {ECO:0000269|PubMed:33219126}; Lipid-anchor {ECO:0000269|PubMed:33219126}.
uniprot
proteins