ID   HMGC2_HUMAN             Reviewed;         370 AA.
AC   Q8TB92; B1AQ42; B3KNV0; B7Z1S7; F8W793; Q6ZSA9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 3.
DT   27-NOV-2024, entry version 166.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic;
DE            EC=4.1.3.4 {ECO:0000269|PubMed:22847177, ECO:0000269|PubMed:22865860};
DE   AltName: Full=3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1;
DE            Short=HMGCL-like 1;
DE   AltName: Full=Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase {ECO:0000303|PubMed:22847177};
DE            Short=er-cHL {ECO:0000303|PubMed:22847177};
GN   Name=HMGCLL1;
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; 3 AND 4).
RC   TISSUE=Brain, and Cerebellum;
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=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 2).
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   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX   PubMed=22865860; DOI=10.1074/jbc.m112.393231;
RA   Montgomery C., Pei Z., Watkins P.A., Miziorko H.M.;
RT   "Identification and characterization of an extramitochondrial human 3-
RT   Hydroxy-3-methylglutaryl-CoA lyase.";
RL   J. Biol. Chem. 287:33227-33236(2012).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF ARG-86; LEU-237 AND HIS-278.
RX   PubMed=22847177; DOI=10.1194/jlr.m025700;
RA   Arnedo M., Menao S., Puisac B., Teresa-Rodrigo M.E., Gil-Rodriguez M.C.,
RA   Lopez-Vinas E., Gomez-Puertas P., Casals N., Casale C.H., Hegardt F.G.,
RA   Pie J.;
RT   "Characterization of a novel HMG-CoA Lyase enzyme with a dual location in
RT   endoplasmic reticulum and cytosol.";
RL   J. Lipid Res. 53:2046-2056(2012).
CC   -!- FUNCTION: Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase
CC       that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-
CC       methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in
CC       ketogenesis, the products of which support energy production in
CC       nonhepatic animal tissues. {ECO:0000269|PubMed:22847177,
CC       ECO:0000269|PubMed:22865860}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC         Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC         ChEBI:CHEBI:57288; EC=4.1.3.4; Evidence={ECO:0000269|PubMed:22847177,
CC         ECO:0000269|PubMed:22865860};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000305|PubMed:22865860};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (at pH 9)
CC         {ECO:0000269|PubMed:22847177};
CC         KM=75 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (at pH 8)
CC         {ECO:0000269|PubMed:22847177};
CC         KM=28 uM for (S)-3-hydroxy-3-methylglutaryl-CoA
CC         {ECO:0000269|PubMed:22865860};
CC         KM=49 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (in presence of
CC         magnesium) {ECO:0000269|PubMed:22865860};
CC         KM=0.18 uM for (S)-3-hydroxy-3-methylglutaryl-CoA (in presence of
CC         manganese) {ECO:0000269|PubMed:22865860};
CC         Vmax=12 nmol/min/mg enzyme with (S)-3-hydroxy-3-methylglutaryl-CoA as
CC         substrate at pH 9 {ECO:0000269|PubMed:22847177};
CC         Vmax=25 nmol/min/mg enzyme with (S)-3-hydroxy-3-methylglutaryl-CoA as
CC         substrate at pH 8 {ECO:0000269|PubMed:22847177};
CC   -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC       methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC       methylglutaryl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22847177}.
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:22847177};
CC       Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8TB92-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TB92-2; Sequence=VSP_033752;
CC       Name=3;
CC         IsoId=Q8TB92-4; Sequence=VSP_038021, VSP_038022;
CC       Name=4;
CC         IsoId=Q8TB92-5; Sequence=VSP_033752, VSP_044324;
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC87045.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAG51462.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR   EMBL; AK055075; BAG51462.1; ALT_SEQ; mRNA.
DR   EMBL; AK127587; BAC87045.1; ALT_FRAME; mRNA.
DR   EMBL; AK293856; BAH11613.1; -; mRNA.
DR   EMBL; AL590290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04442.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX04444.1; -; Genomic_DNA.
DR   EMBL; BC024194; AAH24194.2; -; mRNA.
DR   CCDS; CCDS43474.1; -. [Q8TB92-2]
DR   CCDS; CCDS43475.1; -. [Q8TB92-1]
DR   CCDS; CCDS75473.1; -. [Q8TB92-5]
DR   RefSeq; NP_001035865.1; NM_001042406.1. [Q8TB92-2]
DR   RefSeq; NP_001274670.1; NM_001287741.1. [Q8TB92-5]
DR   RefSeq; NP_001274675.1; NM_001287746.1.
DR   RefSeq; NP_061909.2; NM_019036.2. [Q8TB92-1]
DR   AlphaFoldDB; Q8TB92; -.
DR   SMR; Q8TB92; -.
DR   BioGRID; 120006; 21.
DR   IntAct; Q8TB92; 13.
DR   STRING; 9606.ENSP00000381654; -.
DR   SwissLipids; SLP:000001291; -. [Q8TB92-2]
DR   iPTMnet; Q8TB92; -.
DR   PhosphoSitePlus; Q8TB92; -.
DR   BioMuta; HMGCLL1; -.
DR   DMDM; 189028466; -.
DR   MassIVE; Q8TB92; -.
DR   PaxDb; 9606-ENSP00000381654; -.
DR   PeptideAtlas; Q8TB92; -.
DR   ProteomicsDB; 29914; -.
DR   ProteomicsDB; 73974; -. [Q8TB92-1]
DR   ProteomicsDB; 73975; -. [Q8TB92-2]
DR   Antibodypedia; 31030; 53 antibodies from 13 providers.
DR   DNASU; 54511; -.
DR   Ensembl; ENST00000274901.9; ENSP00000274901.4; ENSG00000146151.14. [Q8TB92-2]
DR   Ensembl; ENST00000308161.8; ENSP00000309737.4; ENSG00000146151.14. [Q8TB92-5]
DR   Ensembl; ENST00000370852.6; ENSP00000359889.2; ENSG00000146151.14. [Q8TB92-4]
DR   Ensembl; ENST00000398661.6; ENSP00000381654.2; ENSG00000146151.14. [Q8TB92-1]
DR   GeneID; 54511; -.
DR   KEGG; hsa:54511; -.
DR   MANE-Select; ENST00000274901.9; ENSP00000274901.4; NM_001042406.2; NP_001035865.1. [Q8TB92-2]
DR   UCSC; uc003pcn.4; human. [Q8TB92-1]
DR   AGR; HGNC:21359; -.
DR   CTD; 54511; -.
DR   DisGeNET; 54511; -.
DR   GeneCards; HMGCLL1; -.
DR   HGNC; HGNC:21359; HMGCLL1.
DR   HPA; ENSG00000146151; Tissue enhanced (brain).
DR   MIM; 619050; gene.
DR   neXtProt; NX_Q8TB92; -.
DR   OpenTargets; ENSG00000146151; -.
DR   PharmGKB; PA134989971; -.
DR   VEuPathDB; HostDB:ENSG00000146151; -.
DR   eggNOG; KOG2368; Eukaryota.
DR   GeneTree; ENSGT00940000159467; -.
DR   HOGENOM; CLU_214024_0_0_1; -.
DR   InParanoid; Q8TB92; -.
DR   OMA; VATAWDC; -.
DR   OrthoDB; 1210873at2759; -.
DR   PhylomeDB; Q8TB92; -.
DR   TreeFam; TF105363; -.
DR   PathwayCommons; Q8TB92; -.
DR   Reactome; R-HSA-77111; Synthesis of Ketone Bodies.
DR   SABIO-RK; Q8TB92; -.
DR   SignaLink; Q8TB92; -.
DR   UniPathway; UPA00896; UER00863.
DR   BioGRID-ORCS; 54511; 39 hits in 1138 CRISPR screens.
DR   ChiTaRS; HMGCLL1; human.
DR   GenomeRNAi; 54511; -.
DR   Pharos; Q8TB92; Tbio.
DR   PRO; PR:Q8TB92; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8TB92; protein.
DR   Bgee; ENSG00000146151; Expressed in cortical plate and 138 other cell types or tissues.
DR   ExpressionAtlas; Q8TB92; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR   GO; GO:0046951; P:ketone body biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006552; P:L-leucine catabolic process; IBA:GO_Central.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   FunFam; 3.20.20.70:FF:000038; Hydroxymethylglutaryl-CoA lyase, mitochondrial; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR043594; HMGL.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42738:SF5; 3-HYDROXY-3-METHYLGLUTARYL-COA LYASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum; Lipid metabolism;
KW   Lipoprotein; Lyase; Membrane; Metal-binding; Myristate;
KW   Proteomics identification; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..370
FT                   /note="3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic"
FT                   /id="PRO_0000334669"
FT   DOMAIN          78..345
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:22865860"
FT   VAR_SEQ         37..66
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033752"
FT   VAR_SEQ         37..53
FT                   /note="TSLLTNLHCFQPDVSGF -> ELQSVMLMLHHGPLRKP (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_038021"
FT   VAR_SEQ         54..370
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_038022"
FT   VAR_SEQ         130..161
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044324"
FT   MUTAGEN         2
FT                   /note="G->A: Abolishes myristoylation and induces a
FT                   subcellular location change."
FT                   /evidence="ECO:0000269|PubMed:22865860"
FT   MUTAGEN         86
FT                   /note="R->Q: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:22847177"
FT   MUTAGEN         237
FT                   /note="L->S: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:22847177"
FT   MUTAGEN         278
FT                   /note="H->R: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:22847177"
FT   CONFLICT        99
FT                   /note="D -> G (in Ref. 1; BAH11613)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  39514 MW;  7DDEE81555E092A1 CRC64;
     MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQTSLL TNLHCFQPDV SGFSVSLAGT
     VACIHWETSQ LSGLPEFVKI VEVGPRDGLQ NEKVIVPTDI KIEFINRLSQ TGLSVIEVTS
     FVSSRWVPQM ADHTEVMKGI HQYPGVRYPV LTPNLQGFHH AVAAGATEIS VFGAASESFS
     KKNINCSIEE SMGKFEEVVK SARHMNIPAR GYVSCALGCP YEGSITPQKV TEVSKRLYGM
     GCYEISLGDT IGVGTPGSMK RMLESVMKEI PPGALAVHCH DTYGQALANI LTALQMGINV
     VDSAVSGLGG CPYAKGASGN VATEDLIYML NGLGLNTGVN LYKVMEAGDF ICKAVNKTTN
     SKVAQASFNA
//