ID   3HIDH_HUMAN             Reviewed;         336 AA.
AC   P31937; Q546Z2; Q9UDN3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   24-JAN-2024, entry version 209.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE            Short=HIBADH;
DE            EC=1.1.1.31;
DE   Flags: Precursor;
GN   Name=HIBADH;
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 [MRNA].
RA   Yuji K., Mitani K., Ueno H., Sato Y., Ikawa S., Hangaishi A., Ogawa S.,
RA   Suzuki T., Nakamoto T., Qiao Y., Hirai H.;
RT   "A new partner gene of the TEL/ETV6, TSL, cloned in acute myeloid leukemia
RT   with t(7;12)(p15;p13).";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L.;
RT   "Cloning and identification of human gene 1 transactivated by hepatitis C
RT   virus NS5A protein.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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 GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   PROTEIN SEQUENCE OF 37-47.
RC   TISSUE=Liver;
RX   PubMed=8313870; DOI=10.1002/elps.11501401181;
RA   Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
RA   Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
RT   "Human liver protein map: update 1993.";
RL   Electrophoresis 14:1216-1222(1993).
RN   [8]
RP   CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX   PubMed=16466957; DOI=10.1016/j.ymgme.2005.09.019;
RA   Loupatty F.J., van der Steen A., Ijlst L., Ruiter J.P., Ofman R.,
RA   Baumgartner M.R., Ballhausen D., Yamaguchi S., Duran M., Wanders R.J.;
RT   "Clinical, biochemical, and molecular findings in three patients with 3-
RT   hydroxyisobutyric aciduria.";
RL   Mol. Genet. Metab. 87:243-248(2006).
RN   [9]
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   [10]
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   [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 (2.38 ANGSTROMS) OF 41-335 OF APOPROTEIN AND IN
RP   COMPLEX WITH NADH.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human hydroxyisobutyrate dehydrogenase.";
RL   Submitted (APR-2006) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC         oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC         ChEBI:CHEBI:57945; EC=1.1.1.31;
CC         Evidence={ECO:0000269|PubMed:16466957};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000269|PubMed:16466957}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P31937; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-11427100, EBI-10225815;
CC       P31937; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-11427100, EBI-11522760;
CC       P31937; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-11427100, EBI-11957045;
CC       P31937; Q99218-1: AMELY; NbExp=3; IntAct=EBI-11427100, EBI-17435683;
CC       P31937; Q92482: AQP3; NbExp=3; IntAct=EBI-11427100, EBI-2808854;
CC       P31937; P07306: ASGR1; NbExp=3; IntAct=EBI-11427100, EBI-1172335;
CC       P31937; O14523: C2CD2L; NbExp=3; IntAct=EBI-11427100, EBI-12822627;
CC       P31937; O95674: CDS2; NbExp=3; IntAct=EBI-11427100, EBI-3913685;
CC       P31937; Q6UVW9: CLEC2A; NbExp=3; IntAct=EBI-11427100, EBI-15839595;
CC       P31937; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-11427100, EBI-2807956;
CC       P31937; Q6PI25: CNIH2; NbExp=3; IntAct=EBI-11427100, EBI-12815321;
CC       P31937; P21964: COMT; NbExp=3; IntAct=EBI-11427100, EBI-372265;
CC       P31937; P52803: EFNA5; NbExp=3; IntAct=EBI-11427100, EBI-1753674;
CC       P31937; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-11427100, EBI-10976398;
CC       P31937; O14653: GOSR2; NbExp=3; IntAct=EBI-11427100, EBI-4401517;
CC       P31937; P21145: MAL; NbExp=3; IntAct=EBI-11427100, EBI-3932027;
CC       P31937; Q9NX14: NDUFB11; NbExp=3; IntAct=EBI-11427100, EBI-1246182;
CC       P31937; P09466: PAEP; NbExp=3; IntAct=EBI-11427100, EBI-465167;
CC       P31937; P26678: PLN; NbExp=3; IntAct=EBI-11427100, EBI-692836;
CC       P31937; Q59EV6: PPGB; NbExp=3; IntAct=EBI-11427100, EBI-14210385;
CC       P31937; O60831: PRAF2; NbExp=3; IntAct=EBI-11427100, EBI-2506064;
CC       P31937; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-11427100, EBI-14199621;
CC       P31937; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-11427100, EBI-10244780;
CC       P31937; Q14108: SCARB2; NbExp=3; IntAct=EBI-11427100, EBI-1564650;
CC       P31937; O75396: SEC22B; NbExp=3; IntAct=EBI-11427100, EBI-1058865;
CC       P31937; O95562: SFT2D2; NbExp=3; IntAct=EBI-11427100, EBI-4402330;
CC       P31937; Q6UX34: SNORC; NbExp=3; IntAct=EBI-11427100, EBI-11957067;
CC       P31937; P02786: TFRC; NbExp=3; IntAct=EBI-11427100, EBI-355727;
CC       P31937; Q9BZW4: TM6SF2; NbExp=3; IntAct=EBI-11427100, EBI-13082040;
CC       P31937; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-11427100, EBI-8638294;
CC       P31937; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-11427100, EBI-347385;
CC       P31937; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-11427100, EBI-2852148;
CC       P31937; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-11427100, EBI-2548832;
CC       P31937; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-11427100, EBI-2819725;
CC       P31937; P63027: VAMP2; NbExp=3; IntAct=EBI-11427100, EBI-520113;
CC       P31937; O95183: VAMP5; NbExp=3; IntAct=EBI-11427100, EBI-10191195;
CC       P31937; O95159: ZFPL1; NbExp=3; IntAct=EBI-11427100, EBI-718439;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Detected in skin fibroblasts.
CC       {ECO:0000269|PubMed:16466957}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC       dehydrogenase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF529362; AAQ09596.1; -; mRNA.
DR   EMBL; AB050000; BAF42045.1; -; mRNA.
DR   EMBL; AK316605; BAG38192.1; -; mRNA.
DR   EMBL; AC007130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236948; EAL24214.1; -; Genomic_DNA.
DR   EMBL; CH471073; EAW93897.1; -; Genomic_DNA.
DR   EMBL; BC032324; AAH32324.1; -; mRNA.
DR   CCDS; CCDS5414.1; -.
DR   RefSeq; NP_689953.1; NM_152740.3.
DR   PDB; 2GF2; X-ray; 2.38 A; A/B/C/D=41-335.
DR   PDB; 2I9P; X-ray; 2.55 A; A/B/C/D=41-336.
DR   PDBsum; 2GF2; -.
DR   PDBsum; 2I9P; -.
DR   AlphaFoldDB; P31937; -.
DR   SMR; P31937; -.
DR   BioGRID; 116289; 90.
DR   IntAct; P31937; 43.
DR   STRING; 9606.ENSP00000265395; -.
DR   ChEMBL; CHEMBL4523215; -.
DR   DrugBank; DB00157; NADH.
DR   GlyGen; P31937; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P31937; -.
DR   PhosphoSitePlus; P31937; -.
DR   SwissPalm; P31937; -.
DR   BioMuta; HIBADH; -.
DR   DMDM; 12643395; -.
DR   CPTAC; CPTAC-520; -.
DR   CPTAC; CPTAC-521; -.
DR   EPD; P31937; -.
DR   jPOST; P31937; -.
DR   MassIVE; P31937; -.
DR   PaxDb; 9606-ENSP00000265395; -.
DR   PeptideAtlas; P31937; -.
DR   ProteomicsDB; 54804; -.
DR   Pumba; P31937; -.
DR   Antibodypedia; 12430; 310 antibodies from 32 providers.
DR   DNASU; 11112; -.
DR   Ensembl; ENST00000265395.7; ENSP00000265395.2; ENSG00000106049.9.
DR   GeneID; 11112; -.
DR   KEGG; hsa:11112; -.
DR   MANE-Select; ENST00000265395.7; ENSP00000265395.2; NM_152740.4; NP_689953.1.
DR   UCSC; uc003szf.4; human.
DR   AGR; HGNC:4907; -.
DR   CTD; 11112; -.
DR   DisGeNET; 11112; -.
DR   GeneCards; HIBADH; -.
DR   HGNC; HGNC:4907; HIBADH.
DR   HPA; ENSG00000106049; Low tissue specificity.
DR   MIM; 608475; gene.
DR   neXtProt; NX_P31937; -.
DR   OpenTargets; ENSG00000106049; -.
DR   PharmGKB; PA29280; -.
DR   VEuPathDB; HostDB:ENSG00000106049; -.
DR   eggNOG; KOG0409; Eukaryota.
DR   GeneTree; ENSGT00940000155255; -.
DR   HOGENOM; CLU_035117_6_0_1; -.
DR   InParanoid; P31937; -.
DR   OMA; MGKKVWH; -.
DR   OrthoDB; 203032at2759; -.
DR   PhylomeDB; P31937; -.
DR   TreeFam; TF314043; -.
DR   PathwayCommons; P31937; -.
DR   Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR   SABIO-RK; P31937; -.
DR   SignaLink; P31937; -.
DR   UniPathway; UPA00362; -.
DR   BioGRID-ORCS; 11112; 16 hits in 1159 CRISPR screens.
DR   ChiTaRS; HIBADH; human.
DR   EvolutionaryTrace; P31937; -.
DR   GeneWiki; 3-hydroxyisobutyrate_dehydrogenase; -.
DR   GenomeRNAi; 11112; -.
DR   Pharos; P31937; Tbio.
DR   PRO; PR:P31937; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P31937; Protein.
DR   Bgee; ENSG00000106049; Expressed in kidney epithelium and 190 other cell types or tissues.
DR   ExpressionAtlas; P31937; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006574; P:valine catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR011548; HIBADH.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01692; HIBADH; 1.
DR   PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR   SWISS-2DPAGE; P31937; -.
DR   Genevisible; P31937; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Branched-chain amino acid catabolism;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:8313870"
FT   CHAIN           37..336
FT                   /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000007158"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000250"
FT   BINDING         40..68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.12"
FT   BINDING         103..104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.12"
FT   BINDING         108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.12"
FT   BINDING         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.12"
FT   BINDING         284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.12"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         60
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         76
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         76
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         95
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         121
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         141
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         145
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         149
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         149
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         238
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         238
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         242
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         242
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         297
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         321
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         321
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           89..95
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           106..114
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           137..149
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           162..168
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          171..177
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           182..189
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          193..201
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           204..232
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           237..245
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           252..256
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           268..271
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   STRAND          275..278
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           279..295
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           301..314
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   TURN            315..317
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:2GF2"
FT   HELIX           326..330
FT                   /evidence="ECO:0007829|PDB:2GF2"
SQ   SEQUENCE   336 AA;  35329 MW;  DA3128774A91AF48 CRC64;
     MAASLRLLGA ASGLRYWSRR LRPAAGSFAA VCSRSVASKT PVGFIGLGNM GNPMAKNLMK
     HGYPLIIYDV FPDACKEFQD AGEQVVSSPA DVAEKADRII TMLPTSINAI EAYSGANGIL
     KKVKKGSLLI DSSTIDPAVS KELAKEVEKM GAVFMDAPVS GGVGAARSGN LTFMVGGVED
     EFAAAQELLG CMGSNVVYCG AVGTGQAAKI CNNMLLAISM IGTAEAMNLG IRLGLDPKLL
     AKILNMSSGR CWSSDTYNPV PGVMDGVPSA NNYQGGFGTT LMAKDLGLAQ DSATSTKSPI
     LLGSLAHQIY RMMCAKGYSK KDFSSVFQFL REEETF
//