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MBLC2_CHICK
ID   MBLC2_CHICK             Reviewed;         277 AA.
AC   Q5F336;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Acyl-coenzyme A thioesterase MBLAC2;
DE            Short=Acyl-CoA thioesterase MBLAC2;
DE            EC=3.1.2.2 {ECO:0000250|UniProtKB:Q68D91};
DE   AltName: Full=Beta-lactamase MBLAC2;
DE            EC=3.5.2.6 {ECO:0000250|UniProtKB:Q68D91};
DE   AltName: Full=Metallo-beta-lactamase domain-containing protein 2;
DE   AltName: Full=Palmitoyl-coenzyme A thioesterase MBLAC2;
GN   Name=MBLAC2; ORFNames=RCJMB04_38d18;
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: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC       the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC       (CoASH), providing the potential to regulate intracellular levels of
CC       acyl-CoAs, free fatty acids and CoASH. Has an acyl-CoA thioesterase
CC       activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA
CC       (hexadecanoyl-CoA; C16:0-CoA). Displays a substrate preference for
CC       fatty acyl-CoAs with chain-lengths C12-C18.
CC       {ECO:0000250|UniProtKB:Q68D91}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC         Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC         Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC         Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q68D91};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q68D91};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q68D91}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q68D91}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q68D91}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q68D91}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000305}.
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DR   EMBL; AJ851814; CAH65448.1; -; mRNA.
DR   RefSeq; NP_001026779.1; NM_001031608.1.
DR   AlphaFoldDB; Q5F336; -.
DR   SMR; Q5F336; -.
DR   STRING; 9031.ENSGALP00000023564; -.
DR   PaxDb; Q5F336; -.
DR   GeneID; 431565; -.
DR   KEGG; gga:431565; -.
DR   CTD; 153364; -.
DR   VEuPathDB; HostDB:geneid_431565; -.
DR   eggNOG; KOG0813; Eukaryota.
DR   HOGENOM; CLU_030571_0_2_1; -.
DR   InParanoid; Q5F336; -.
DR   OrthoDB; 1203911at2759; -.
DR   PhylomeDB; Q5F336; -.
DR   PRO; PR:Q5F336; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:RHEA.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endoplasmic reticulum; Fatty acid metabolism; Hydrolase;
KW   Lipid metabolism; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW   Reference proteome; Zinc.
FT   CHAIN           1..277
FT                   /note="Acyl-coenzyme A thioesterase MBLAC2"
FT                   /id="PRO_0000325937"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q68D91"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q68D91"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  30774 MW;  EC3665A739B052FA CRC64;
     MSALEWFAHK PLGSGIFWIQ ERFYESGNRA NIWLVRGSQR DLVIDAGLGL RSLPDYLRAA
     GLLAPPDGAG PRPLLAVATH VHFDHSGGLQ HFEEVAVHSA EAAALLRGDN YEAVTWLSDR
     EVTRPPRPGW RARHFCVPPV RPSRLLQEGD VISLGDRQLT VMHMPGHSRG SICLHDREHK
     ILFSGDVVYD GSMIDWLPYS NVSDYVVSCQ RLMELVDRGL VEKVLPGHFN MFGAERLYRL
     ASNYISKAGI CHKVSTCAMR SIASIALHLT NSRGTSS
 
 
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