FAHD1_HUMAN
ID FAHD1_HUMAN Reviewed; 224 AA.
AC Q6P587; B1AK40; B1AK41; Q6FIC7; Q96RY1; Q9H0N6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Acylpyruvase FAHD1, mitochondrial;
DE EC=3.7.1.5 {ECO:0000269|PubMed:21878618};
DE AltName: Full=Fumarylacetoacetate hydrolase domain-containing protein 1;
DE Short=FAH domain-containing protein 1;
DE AltName: Full=Oxaloacetate decarboxylase;
DE Short=OAA decarboxylase;
DE EC=4.1.1.112 {ECO:0000269|PubMed:25575590};
DE AltName: Full=YisK-like protein;
DE Flags: Precursor;
GN Name=FAHD1; Synonyms=C16orf36, YISKL;
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 GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Glial tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP CATALYTIC ACTIVITY, KINETIC PARAMETERS, COFACTOR, MUTAGENESIS OF ASP-102
RP AND ARG-106, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21878618; DOI=10.1074/jbc.m111.264770;
RA Pircher H., Straganz G.D., Ehehalt D., Morrow G., Tanguay R.M.,
RA Jansen-Durr P.;
RT "Identification of human fumarylacetoacetate hydrolase domain containing
RT protein 1 (FAHD1) as a novel mitochondrial acylpyruvase.";
RL J. Biol. Chem. 286:36500-36508(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-30; GLU-33; ASP-102 AND ARG-106.
RX PubMed=25575590; DOI=10.1074/jbc.m114.609305;
RA Pircher H., von Grafenstein S., Diener T., Metzger C., Albertini E.,
RA Taferner A., Unterluggauer H., Kramer C., Liedl K.R., Jansen-Durr P.;
RT "Identification of FAH domain containing protein 1 (FAHD1) as oxaloacetate
RT decarboxylase.";
RL J. Biol. Chem. 290:6755-6762(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP AND DIMERIZATION.
RX PubMed=15551868; DOI=10.1515/bc.2004.122;
RA Manjasetty B.A., Niesen F.H., Delbrueck H., Goetz F., Sievert V.,
RA Buessow K., Behlke J., Heinemann U.;
RT "X-ray structure of fumarylacetoacetate hydrolase family member Homo
RT sapiens FLJ36880.";
RL Biol. Chem. 385:935-942(2004).
CC -!- FUNCTION: Probable mitochondrial acylpyruvase which is able to
CC hydrolyze acetylpyruvate and fumarylpyruvate in vitro (PubMed:15551868,
CC PubMed:21878618). Also has oxaloacetate decarboxylase activity
CC (PubMed:25575590). {ECO:0000269|PubMed:15551868,
CC ECO:0000269|PubMed:21878618, ECO:0000269|PubMed:25575590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate;
CC Xref=Rhea:RHEA:19009, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:57278; EC=3.7.1.5;
CC Evidence={ECO:0000269|PubMed:21878618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=4.1.1.112;
CC Evidence={ECO:0000269|PubMed:25575590};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:15551868, ECO:0000305|PubMed:21878618};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:15551868, ECO:0000305|PubMed:21878618};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for acetylpyruvate {ECO:0000269|PubMed:21878618};
CC KM=32 uM for oxaloacetate {ECO:0000269|PubMed:25575590};
CC Vmax=0.135 umol/min/mg enzyme toward acetylpyruvate
CC {ECO:0000269|PubMed:21878618};
CC Vmax=0.21 umol/min/mg enzyme with oxaloacetate as substrate
CC {ECO:0000269|PubMed:25575590};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15551868}.
CC -!- INTERACTION:
CC Q6P587-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-12902289, EBI-752094;
CC Q6P587-2; P04792: HSPB1; NbExp=3; IntAct=EBI-12902289, EBI-352682;
CC Q6P587-2; P07196: NEFL; NbExp=3; IntAct=EBI-12902289, EBI-475646;
CC Q6P587-2; P60891: PRPS1; NbExp=3; IntAct=EBI-12902289, EBI-749195;
CC Q6P587-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12902289, EBI-396669;
CC Q6P587-2; O76024: WFS1; NbExp=3; IntAct=EBI-12902289, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21878618}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:21878618}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P587-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P587-2; Sequence=VSP_013741;
CC Name=3;
CC IsoId=Q6P587-3; Sequence=VSP_046259;
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
CC {ECO:0000269|PubMed:21878618}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK61295.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006639; AAK61295.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL136720; CAB66654.1; -; mRNA.
DR EMBL; AK094199; BAC04308.1; -; mRNA.
DR EMBL; CR533499; CAG38530.1; -; mRNA.
DR EMBL; AC012180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063017; AAH63017.1; -; mRNA.
DR RefSeq; NP_001018114.1; NM_001018104.2. [Q6P587-3]
DR RefSeq; NP_001135870.1; NM_001142398.1. [Q6P587-2]
DR RefSeq; NP_112485.1; NM_031208.3. [Q6P587-1]
DR PDB; 1SAW; X-ray; 2.20 A; A/B=2-224.
DR PDB; 6FOG; X-ray; 1.94 A; A/B/C/D/E/F/G/H=1-224.
DR PDB; 6FOH; X-ray; 1.56 A; A/B=1-224.
DR PDBsum; 1SAW; -.
DR PDBsum; 6FOG; -.
DR PDBsum; 6FOH; -.
DR AlphaFoldDB; Q6P587; -.
DR SMR; Q6P587; -.
DR BioGRID; 123622; 197.
DR IntAct; Q6P587; 22.
DR MINT; Q6P587; -.
DR STRING; 9606.ENSP00000372112; -.
DR ChEMBL; CHEMBL4523346; -.
DR iPTMnet; Q6P587; -.
DR PhosphoSitePlus; Q6P587; -.
DR BioMuta; FAHD1; -.
DR DMDM; 68566321; -.
DR UCD-2DPAGE; Q6P587; -.
DR EPD; Q6P587; -.
DR jPOST; Q6P587; -.
DR MassIVE; Q6P587; -.
DR MaxQB; Q6P587; -.
DR PaxDb; Q6P587; -.
DR PeptideAtlas; Q6P587; -.
DR PRIDE; Q6P587; -.
DR ProteomicsDB; 3012; -.
DR ProteomicsDB; 66992; -. [Q6P587-1]
DR ProteomicsDB; 66993; -. [Q6P587-2]
DR Antibodypedia; 56108; 68 antibodies from 14 providers.
DR DNASU; 81889; -.
DR Ensembl; ENST00000382666.6; ENSP00000372112.5; ENSG00000180185.12.
DR Ensembl; ENST00000382668.8; ENSP00000372114.5; ENSG00000180185.12.
DR Ensembl; ENST00000427358.4; ENSP00000398053.3; ENSG00000180185.12.
DR GeneID; 81889; -.
DR KEGG; hsa:81889; -.
DR UCSC; uc002cnc.2; human. [Q6P587-1]
DR CTD; 81889; -.
DR DisGeNET; 81889; -.
DR GeneCards; FAHD1; -.
DR HGNC; HGNC:14169; FAHD1.
DR HPA; ENSG00000180185; Tissue enhanced (kidney).
DR MalaCards; FAHD1; -.
DR MIM; 616320; gene.
DR neXtProt; NX_Q6P587; -.
DR PharmGKB; PA25551; -.
DR VEuPathDB; HostDB:ENSG00000180185; -.
DR eggNOG; KOG1535; Eukaryota.
DR HOGENOM; CLU_028458_5_0_1; -.
DR InParanoid; Q6P587; -.
DR OMA; YALSIDM; -.
DR OrthoDB; 1216556at2759; -.
DR PhylomeDB; Q6P587; -.
DR TreeFam; TF300911; -.
DR BRENDA; 3.7.1.5; 2681.
DR BRENDA; 4.1.1.112; 2681.
DR PathwayCommons; Q6P587; -.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; Q6P587; -.
DR SignaLink; Q6P587; -.
DR BioGRID-ORCS; 81889; 13 hits in 1080 CRISPR screens.
DR ChiTaRS; FAHD1; human.
DR EvolutionaryTrace; Q6P587; -.
DR GeneWiki; FAHD1; -.
DR GenomeRNAi; 81889; -.
DR Pharos; Q6P587; Tbio.
DR PRO; PR:Q6P587; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6P587; protein.
DR Bgee; ENSG00000180185; Expressed in kidney epithelium and 192 other tissues.
DR Genevisible; Q6P587; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0018773; F:acetylpyruvate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0047621; F:acylpyruvate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0034545; F:fumarylpyruvate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IDA:UniProtKB.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium; Cytoplasm;
KW Hydrolase; Lyase; Magnesium; Metal-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..224
FT /note="Acylpyruvase FAHD1, mitochondrial"
FT /id="PRO_0000156829"
FT BINDING 71
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15551868"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15551868"
FT BINDING 102
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15551868"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYQ8"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0F8"
FT MOD_RES 115
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0F8"
FT VAR_SEQ 213..224
FT /note="VSMTFKVEKPEY -> PKVSSATLPVRLQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013741"
FT VAR_SEQ 213..224
FT /note="VSMTFKVEKPEY -> RQGLTLSPKLECSSAITAHCSLELPGSSNPPSASRF
FT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046259"
FT VARIANT 110
FT /note="D -> N (in dbSNP:rs3743853)"
FT /id="VAR_049014"
FT MUTAGEN 30
FT /note="H->A: Impaired oxaloacetate decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:25575590"
FT MUTAGEN 33
FT /note="E->A: Impaired oxaloacetate decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:25575590"
FT MUTAGEN 102
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-106."
FT /evidence="ECO:0000269|PubMed:21878618,
FT ECO:0000269|PubMed:25575590"
FT MUTAGEN 106
FT /note="R->A: Loss of catalytic activity; when associated
FT with A-102."
FT /evidence="ECO:0000269|PubMed:21878618,
FT ECO:0000269|PubMed:25575590"
FT CONFLICT 177
FT /note="S -> P (in Ref. 4; CAG38530)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6FOH"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6FOH"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6FOH"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:6FOH"
SQ SEQUENCE 224 AA; 24843 MW; A005E4ECD613C72E CRC64;
MGIMAASRPL SRFWEWGKNI VCVGRNYADH VREMRSAVLS EPVLFLKPST AYAPEGSPIL
MPAYTRNLHH ELELGVVMGK RCRAVPEAAA MDYVGGYALC LDMTARDVQD ECKKKGLPWT
LAKSFTASCP VSAFVPKEKI PDPHKLKLWL KVNGELRQEG ETSSMIFSIP YIISYVSKII
TLEEGDIILT GTPKGVGPVK ENDEIEAGIH GLVSMTFKVE KPEY
