MBLC2_HUMAN
ID MBLC2_HUMAN Reviewed; 279 AA.
AC Q68D91; D6RJI1; Q8IY16; Q8N8D8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Acyl-coenzyme A thioesterase MBLAC2;
DE Short=Acyl-CoA thioesterase MBLAC2;
DE EC=3.1.2.2 {ECO:0000269|PubMed:33219126};
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000269|PubMed:31434986};
DE AltName: Full=Metallo-beta-lactamase domain-containing protein 2;
DE AltName: Full=Palmitoyl-coenzyme A thioesterase MBLAC2;
GN Name=MBLAC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-128.
RC TISSUE=Brain, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-128.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-128.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-279 (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=31434986; DOI=10.1038/s41598-019-48723-y;
RA Diene S.M., Pinault L., Keshri V., Armstrong N., Khelaifia S.,
RA Chabriere E., Caetano-Anolles G., Colson P., La Scola B., Rolain J.M.,
RA Pontarotti P., Raoult D.;
RT "Human metallo-beta-lactamase enzymes degrade penicillin.";
RL Sci. Rep. 9:12173-12173(2019).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PALMITOYLATION AT
RP CYS-254, AND MUTAGENESIS OF ASP-87; HIS-88; SER-89; TYR-93; CYS-176;
RP CYS-212 AND CYS-254.
RX PubMed=33219126; DOI=10.1074/jbc.ra120.015701;
RA Malgapo M.I.P., Safadi J.M., Linder M.E.;
RT "Metallo-beta-Lactamase Domain-Containing Protein 2 (MBLAC2) is S-
RT palmitoylated and exhibits acyl-CoA hydrolase activity.";
RL J. Biol. Chem. 296:100106-100118(2021).
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 (PubMed:33219126). Has an acyl-
CC CoA thioesterase activity towards the long chain fatty acyl-CoA
CC thioester palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA)
CC (PubMed:33219126). Displays a substrate preference for fatty acyl-CoAs
CC with chain-lengths C12-C18 (PubMed:33219126). Possesses beta-lactamase
CC activity, catalyzing the hydrolysis of penicillin G and nitrocefin
CC (PubMed:31434986). Exhibits no activity towards other beta-lactam
CC antibiotic classes including cephalosporins (cefotaxime) and
CC carbapenems (imipenem) (PubMed:31434986). {ECO:0000269|PubMed:31434986,
CC ECO:0000269|PubMed:33219126}.
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:0000269|PubMed:33219126};
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:0000269|PubMed:33219126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:33219126};
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:0000269|PubMed:33219126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:33219126};
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:0000269|PubMed:33219126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:33219126};
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:0000269|PubMed:31434986};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:33219126};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305|PubMed:33219126};
CC -!- ACTIVITY REGULATION: Beta-lactamase activity is inhibited by sulbactam.
CC {ECO:0000269|PubMed:31434986}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for palmitoyl-CoA {ECO:0000269|PubMed:33219126};
CC KM=370 uM for nitrocefin {ECO:0000269|PubMed:31434986};
CC Vmax=102.5 nmol/min/mg enzyme towards palmitoyl-CoA
CC {ECO:0000269|PubMed:33219126};
CC -!- INTERACTION:
CC Q68D91; Q96AL5: PBX3; NbExp=3; IntAct=EBI-21018038, EBI-741171;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:33219126}; Lipid-anchor
CC {ECO:0000269|PubMed:33219126}. Cell membrane
CC {ECO:0000269|PubMed:33219126}; Lipid-anchor
CC {ECO:0000269|PubMed:33219126}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68D91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68D91-2; Sequence=VSP_032490;
CC -!- PTM: Palmitoylated on Cys-254 by ZDHHC20.
CC {ECO:0000269|PubMed:33219126}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AK096942; BAC04908.1; -; mRNA.
DR EMBL; AK289778; BAF82467.1; -; mRNA.
DR EMBL; AC093510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95979.1; -; Genomic_DNA.
DR EMBL; BC038230; AAH38230.1; -; mRNA.
DR EMBL; CR749512; CAH18329.1; -; mRNA.
DR CCDS; CCDS4067.1; -. [Q68D91-1]
DR RefSeq; NP_981951.1; NM_203406.1. [Q68D91-1]
DR AlphaFoldDB; Q68D91; -.
DR SMR; Q68D91; -.
DR BioGRID; 127492; 69.
DR IntAct; Q68D91; 35.
DR MINT; Q68D91; -.
DR STRING; 9606.ENSP00000314776; -.
DR iPTMnet; Q68D91; -.
DR PhosphoSitePlus; Q68D91; -.
DR SwissPalm; Q68D91; -.
DR BioMuta; MBLAC2; -.
DR DMDM; 311033427; -.
DR EPD; Q68D91; -.
DR jPOST; Q68D91; -.
DR MassIVE; Q68D91; -.
DR MaxQB; Q68D91; -.
DR PaxDb; Q68D91; -.
DR PeptideAtlas; Q68D91; -.
DR PRIDE; Q68D91; -.
DR ProteomicsDB; 66062; -. [Q68D91-1]
DR ProteomicsDB; 66063; -. [Q68D91-2]
DR Antibodypedia; 50739; 18 antibodies from 8 providers.
DR DNASU; 153364; -.
DR Ensembl; ENST00000316610.7; ENSP00000314776.6; ENSG00000176055.10. [Q68D91-1]
DR Ensembl; ENST00000514906.1; ENSP00000425600.1; ENSG00000176055.10. [Q68D91-2]
DR GeneID; 153364; -.
DR KEGG; hsa:153364; -.
DR MANE-Select; ENST00000316610.7; ENSP00000314776.6; NM_203406.2; NP_981951.2.
DR UCSC; uc003kjp.3; human. [Q68D91-1]
DR CTD; 153364; -.
DR GeneCards; MBLAC2; -.
DR HGNC; HGNC:33711; MBLAC2.
DR HPA; ENSG00000176055; Low tissue specificity.
DR neXtProt; NX_Q68D91; -.
DR OpenTargets; ENSG00000176055; -.
DR PharmGKB; PA164722236; -.
DR VEuPathDB; HostDB:ENSG00000176055; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00390000017819; -.
DR HOGENOM; CLU_030571_0_2_1; -.
DR InParanoid; Q68D91; -.
DR OMA; VASHTHF; -.
DR OrthoDB; 1203911at2759; -.
DR PhylomeDB; Q68D91; -.
DR TreeFam; TF319889; -.
DR PathwayCommons; Q68D91; -.
DR SignaLink; Q68D91; -.
DR BioGRID-ORCS; 153364; 6 hits in 1072 CRISPR screens.
DR ChiTaRS; MBLAC2; human.
DR GenomeRNAi; 153364; -.
DR Pharos; Q68D91; Tdark.
DR PRO; PR:Q68D91; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q68D91; protein.
DR Bgee; ENSG00000176055; Expressed in endothelial cell and 169 other tissues.
DR Genevisible; Q68D91; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008800; F:beta-lactamase activity; IDA: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; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..279
FT /note="Acyl-coenzyme A thioesterase MBLAC2"
FT /id="PRO_0000325935"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:33219126"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:33219126"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT LIPID 254
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:33219126"
FT VAR_SEQ 153..279
FT /note="DVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSR
FT ISDYVGTCERLIELVDRGLVEKVLPGHFNTFGAERLFRLASNYISKAGICHKVSTFAMR
FT SLASLALRVTNSRTSP -> NGPPRARALVKGGYWEETVRVPHVADLRGHKGDYFGTSQ
FT SHFCFTLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032490"
FT VARIANT 128
FT /note="T -> A (in dbSNP:rs2162986)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_039956"
FT MUTAGEN 87
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:33219126"
FT MUTAGEN 88
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:33219126"
FT MUTAGEN 89
FT /note="S->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:33219126"
FT MUTAGEN 93
FT /note="Y->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:33219126"
FT MUTAGEN 176
FT /note="C->A: No effect on ZDHH20-catalyzed palmitoylation."
FT /evidence="ECO:0000269|PubMed:33219126"
FT MUTAGEN 212
FT /note="C->A: No effect on ZDHH20-catalyzed palmitoylation."
FT /evidence="ECO:0000269|PubMed:33219126"
FT MUTAGEN 254
FT /note="C->A: Loss of ZDHH20-catalyzed palmitoylation. Shows
FT only a slight reduction in the Vmax and a small increase in
FT the Km towards palmitoyl-CoA in comparison with wild-type."
FT /evidence="ECO:0000269|PubMed:33219126"
FT CONFLICT 25
FT /note="E -> G (in Ref. 1; BAC04908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 31372 MW; 14C9C03B62C81867 CRC64;
MSALEWYAHK SLGDGIFWIQ ERFYESGNRA NIWLVRGSEQ DVVIDTGLGL RSLPEYLYSS
GLLQDREAKE DAARRPLLAV ATHVHFDHSG GLYQFDRVAV HHAEAEALAR GDNFETVTWL
SDSEVVRTPS PGWRARQFRV QAVQPTLILQ DGDVINLGDR QLTVMHMPGH SRGSICLHDK
DRKILFSGDV VYDGSLIDWL PYSRISDYVG TCERLIELVD RGLVEKVLPG HFNTFGAERL
FRLASNYISK AGICHKVSTF AMRSLASLAL RVTNSRTSP
