ID   NNTM_HUMAN              Reviewed;        1086 AA.
AC   Q13423; Q16796; Q2TB60; Q8N3V4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=NAD(P) transhydrogenase, mitochondrial;
DE            EC=7.1.1.1 {ECO:0000250|UniProtKB:Q2RSB2};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase;
DE   AltName: Full=Pyridine nucleotide transhydrogenase;
DE   Flags: Precursor;
GN   Name=NNT;
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].
RX   PubMed=9524818; DOI=10.3109/10425179709034058;
RA   Ware J., Zieger B.;
RT   "Cloning and deduced amino acid sequence of human nicotinamide nucleotide
RT   transhydrogenase.";
RL   DNA Seq. 7:369-374(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=8616157; DOI=10.1016/0005-2728(95)00159-x;
RA   Lagberg E.M., Betsholtz C., Rydstrom J.;
RT   "The cDNA sequence of proton-pumping nicotinamide nucleotide
RT   transhydrogenase from man and mouse.";
RL   Biochim. Biophys. Acta 1273:203-205(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-397, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [6]
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   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND VARIANTS GCCD4 ASN-193; ALA-357; PRO-365;
RP   LEU-437; VAL-533; ARG-664; ARG-678; ASP-862; PRO-977; PRO-1008 AND
RP   LYS-1009.
RX   PubMed=22634753; DOI=10.1038/ng.2299;
RA   Meimaridou E., Kowalczyk J., Guasti L., Hughes C.R., Wagner F.,
RA   Frommolt P., Nurnberg P., Mann N.P., Banerjee R., Saka H.N., Chapple J.P.,
RA   King P.J., Clark A.J., Metherell L.A.;
RT   "Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause
RT   familial glucocorticoid deficiency.";
RL   Nat. Genet. 44:740-742(2012).
RN   [8]
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   [9]
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 880-1086 IN COMPLEX WITH NADP.
RX   PubMed=10673423; DOI=10.1016/s0969-2126(00)00075-7;
RA   White S.A., Peake S.J., McSweeney S., Leonard G., Cotton N.P.J.,
RA   Jackson J.B.;
RT   "The high-resolution structure of the NADP(H)-binding component (dIII) of
RT   proton-translocating transhydrogenase from human heart mitochondria.";
RL   Structure 8:1-12(2000).
RN   [11] {ECO:0007744|PDB:1PT9}
RP   X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 880-1086 IN COMPLEX WITH
RP   SUBSTRATE ANALOG.
RX   PubMed=12791694; DOI=10.1074/jbc.m303061200;
RA   Singh A., Venning J.D., Quirk P.G., van Boxel G.I., Rodrigues D.J.,
RA   White S.A., Jackson J.B.;
RT   "Interactions between transhydrogenase and thio-nicotinamide Analogues of
RT   NAD(H) and NADP(H) underline the importance of nucleotide conformational
RT   changes in coupling to proton translocation.";
RL   J. Biol. Chem. 278:33208-33216(2003).
RN   [12] {ECO:0007744|PDB:1U31}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 880-1086 IN COMPLEX WITH NADP.
RX   PubMed=15323555; DOI=10.1021/bi0497594;
RA   Mather O.C., Singh A., van Boxel G.I., White S.A., Jackson J.B.;
RT   "Active-site conformational changes associated with hydride transfer in
RT   proton-translocating transhydrogenase.";
RL   Biochemistry 43:10952-10964(2004).
CC   -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC       respiration and ATP hydrolysis and functions as a proton pump across
CC       the membrane (By similarity). May play a role in reactive oxygen
CC       species (ROS) detoxification in the adrenal gland (PubMed:22634753).
CC       {ECO:0000250|UniProtKB:P07001, ECO:0000269|PubMed:22634753}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC         Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC         Evidence={ECO:0000250|UniProtKB:Q2RSB2};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11024}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with expression most readily
CC       detectable in adrenal, heart, kidney, thyroid and adipose tissues.
CC       {ECO:0000269|PubMed:22634753}.
CC   -!- DISEASE: Glucocorticoid deficiency 4 with or without mineralocorticoid
CC       deficiency (GCCD4) [MIM:614736]: A form of glucocorticoid deficiency, a
CC       rare autosomal recessive disorder characterized by resistance to ACTH
CC       action on the adrenal cortex, adrenal insufficiency and an inability of
CC       the adrenal cortex to produce cortisol. It usually presents in the
CC       neonatal period or in early childhood with episodes of hypoglycemia and
CC       other symptoms related to cortisol deficiency, including failure to
CC       thrive, recurrent illnesses or infections, convulsions, and shock. In a
CC       small number of patients hypoglycemia can be sufficiently severe and
CC       persistent that it leads to serious long-term neurological damage or
CC       death. The diagnosis is readily confirmed with a low plasma cortisol
CC       measurement in the presence of an elevated ACTH level, and normal
CC       aldosterone and plasma renin measurements.
CC       {ECO:0000269|PubMed:22634753}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PNT beta subunit
CC       family. {ECO:0000305}.
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DR   EMBL; U40490; AAC51914.1; -; mRNA.
DR   EMBL; Z50101; CAA90428.1; -; mRNA.
DR   EMBL; AL831822; CAD38536.1; -; mRNA.
DR   EMBL; BC110543; AAI10544.1; -; mRNA.
DR   CCDS; CCDS3949.1; -.
DR   PIR; G02257; G02257.
DR   RefSeq; NP_036475.3; NM_012343.3.
DR   RefSeq; NP_892022.2; NM_182977.2.
DR   RefSeq; XP_005248331.1; XM_005248274.4.
DR   RefSeq; XP_011512303.1; XM_011514001.2.
DR   RefSeq; XP_016864782.1; XM_017009293.1.
DR   PDB; 1DJL; X-ray; 2.00 A; A/B=880-1086.
DR   PDB; 1PT9; X-ray; 2.42 A; A/B=880-1086.
DR   PDB; 1U31; X-ray; 2.20 A; A/B=880-1086.
DR   PDBsum; 1DJL; -.
DR   PDBsum; 1PT9; -.
DR   PDBsum; 1U31; -.
DR   AlphaFoldDB; Q13423; -.
DR   SMR; Q13423; -.
DR   BioGRID; 117076; 191.
DR   IntAct; Q13423; 37.
DR   MINT; Q13423; -.
DR   STRING; 9606.ENSP00000264663; -.
DR   DrugBank; DB01763; 7-thionicotinamide-adenine-dinucleotide phosphate.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR   DrugBank; DB09072; Sodium oxybate.
DR   DrugBank; DB09092; Xanthinol.
DR   CarbonylDB; Q13423; -.
DR   GlyGen; Q13423; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13423; -.
DR   MetOSite; Q13423; -.
DR   PhosphoSitePlus; Q13423; -.
DR   SwissPalm; Q13423; -.
DR   BioMuta; NNT; -.
DR   DMDM; 51338801; -.
DR   EPD; Q13423; -.
DR   jPOST; Q13423; -.
DR   MassIVE; Q13423; -.
DR   MaxQB; Q13423; -.
DR   PaxDb; 9606-ENSP00000264663; -.
DR   PeptideAtlas; Q13423; -.
DR   ProteomicsDB; 59408; -.
DR   Pumba; Q13423; -.
DR   Antibodypedia; 1369; 178 antibodies from 29 providers.
DR   DNASU; 23530; -.
DR   Ensembl; ENST00000264663.9; ENSP00000264663.5; ENSG00000112992.18.
DR   Ensembl; ENST00000344920.9; ENSP00000343873.4; ENSG00000112992.18.
DR   Ensembl; ENST00000653251.1; ENSP00000499281.1; ENSG00000112992.18.
DR   Ensembl; ENST00000656666.1; ENSP00000499249.1; ENSG00000112992.18.
DR   Ensembl; ENST00000662525.1; ENSP00000499639.1; ENSG00000112992.18.
DR   Ensembl; ENST00000669601.1; ENSP00000499527.1; ENSG00000112992.18.
DR   Ensembl; ENST00000670904.1; ENSP00000499611.1; ENSG00000112992.18.
DR   Ensembl; ENST00000671668.1; ENSP00000499494.1; ENSG00000112992.18.
DR   GeneID; 23530; -.
DR   KEGG; hsa:23530; -.
DR   MANE-Select; ENST00000344920.9; ENSP00000343873.4; NM_182977.3; NP_892022.2.
DR   UCSC; uc003joe.4; human.
DR   AGR; HGNC:7863; -.
DR   CTD; 23530; -.
DR   DisGeNET; 23530; -.
DR   GeneCards; NNT; -.
DR   HGNC; HGNC:7863; NNT.
DR   HPA; ENSG00000112992; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; NNT; -.
DR   MIM; 607878; gene.
DR   MIM; 614736; phenotype.
DR   neXtProt; NX_Q13423; -.
DR   OpenTargets; ENSG00000112992; -.
DR   Orphanet; 361; Familial glucocorticoid deficiency.
DR   PharmGKB; PA31667; -.
DR   VEuPathDB; HostDB:ENSG00000112992; -.
DR   eggNOG; ENOG502QQ0A; Eukaryota.
DR   GeneTree; ENSGT00390000004624; -.
DR   HOGENOM; CLU_003376_1_0_1; -.
DR   InParanoid; Q13423; -.
DR   OMA; EQCREVD; -.
DR   OrthoDB; 313696at2759; -.
DR   PhylomeDB; Q13423; -.
DR   TreeFam; TF300636; -.
DR   BioCyc; MetaCyc:HS03639-MONOMER; -.
DR   BRENDA; 1.6.1.2; 2681.
DR   BRENDA; 7.1.1.1; 2681.
DR   PathwayCommons; Q13423; -.
DR   Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR   SignaLink; Q13423; -.
DR   BioGRID-ORCS; 23530; 16 hits in 1165 CRISPR screens.
DR   ChiTaRS; NNT; human.
DR   EvolutionaryTrace; Q13423; -.
DR   GeneWiki; NNT_(gene); -.
DR   GenomeRNAi; 23530; -.
DR   Pharos; Q13423; Tbio.
DR   PRO; PR:Q13423; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q13423; Protein.
DR   Bgee; ENSG00000112992; Expressed in heart right ventricle and 194 other cell types or tissues.
DR   ExpressionAtlas; Q13423; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB.
DR   GO; GO:0005746; C:mitochondrial respirasome; TAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR   GO; GO:0051287; F:NAD binding; TAS:UniProtKB.
DR   GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; TAS:UniProtKB.
DR   GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IEA:Ensembl.
DR   GO; GO:0032364; P:intracellular oxygen homeostasis; IEA:Ensembl.
DR   GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; IEA:Ensembl.
DR   GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:1902600; P:proton transmembrane transport; TAS:UniProtKB.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
DR   GO; GO:0033273; P:response to vitamin; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB.
DR   CDD; cd05304; Rubrum_tdh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR008142; AlaDH/PNT_CS1.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR026255; NADP_transhyd_a.
DR   InterPro; IPR024605; NADP_transhyd_a_C.
DR   InterPro; IPR034300; PNTB-like.
DR   NCBIfam; TIGR00561; pntA; 1.
DR   PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR   PANTHER; PTHR10160:SF22; NAD(P) TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   Pfam; PF02233; PNTB; 1.
DR   Pfam; PF12769; PNTB_4TM; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00836; ALADH_PNT_1; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
DR   Genevisible; Q13423; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; NADP; Nucleotide-binding;
KW   Reference proteome; Transit peptide; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P11024"
FT   CHAIN           44..1086
FT                   /note="NAD(P) transhydrogenase, mitochondrial"
FT                   /id="PRO_0000001055"
FT   TOPO_DOM        44..474
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P11024"
FT   TRANSMEM        475..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        527..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        558..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        579..595
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P11024"
FT   TRANSMEM        596..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        646..666
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        672..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        702..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        723..739
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P11024"
FT   TRANSMEM        740..760
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        778..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        801..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        833..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        857..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        880..1086
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P11024"
FT   BINDING         182..184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07001"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07001"
FT   BINDING         257..259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07001"
FT   BINDING         287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:W5PFI3"
FT   BINDING         300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07001"
FT   BINDING         319
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07001"
FT   BINDING         933
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10673423,
FT                   ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT                   ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT                   ECO:0007744|PDB:1U31"
FT   BINDING         965..970
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10673423,
FT                   ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT                   ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT                   ECO:0007744|PDB:1U31"
FT   BINDING         1007..1011
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10673423,
FT                   ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT                   ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT                   ECO:0007744|PDB:1U31"
FT   BINDING         1026..1027
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10673423,
FT                   ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1DJL,
FT                   ECO:0007744|PDB:1U31"
FT   BINDING         1042..1049
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10673423,
FT                   ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT                   ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT                   ECO:0007744|PDB:1U31"
FT   BINDING         1068..1069
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10673423,
FT                   ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT                   ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT                   ECO:0007744|PDB:1U31"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         117
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61941"
FT   MOD_RES         224
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61941"
FT   MOD_RES         294
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61941"
FT   MOD_RES         331
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61941"
FT   MOD_RES         397
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1079
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61941"
FT   VARIANT         193
FT                   /note="S -> N (in GCCD4; dbSNP:rs867004061)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068781"
FT   VARIANT         357
FT                   /note="T -> A (in GCCD4; dbSNP:rs1447408865)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068782"
FT   VARIANT         365
FT                   /note="H -> P (in GCCD4)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068783"
FT   VARIANT         437
FT                   /note="P -> L (in GCCD4; dbSNP:rs781183677)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068784"
FT   VARIANT         533
FT                   /note="A -> V (in GCCD4; dbSNP:rs387907232)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068785"
FT   VARIANT         664
FT                   /note="G -> R (in GCCD4; dbSNP:rs371979800)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068786"
FT   VARIANT         678
FT                   /note="G -> R (in GCCD4)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068787"
FT   VARIANT         862
FT                   /note="G -> D (in GCCD4; dbSNP:rs1474421419)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068788"
FT   VARIANT         977
FT                   /note="L -> P (in GCCD4; dbSNP:rs387907233)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068789"
FT   VARIANT         1008
FT                   /note="A -> P (in GCCD4; dbSNP:rs387907234)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068790"
FT   VARIANT         1009
FT                   /note="N -> K (in GCCD4; dbSNP:rs370273690)"
FT                   /evidence="ECO:0000269|PubMed:22634753"
FT                   /id="VAR_068791"
FT   CONFLICT        176
FT                   /note="A -> T (in Ref. 2; CAA90428)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="G -> E (in Ref. 3; CAD38536)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="A -> E (in Ref. 1; AAC51914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="A -> S (in Ref. 1; AAC51914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        706
FT                   /note="F -> S (in Ref. 1; AAC51914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        731
FT                   /note="T -> P (in Ref. 1; AAC51914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        810
FT                   /note="S -> A (in Ref. 2; CAA90428)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        824
FT                   /note="A -> P (in Ref. 2; CAA90428)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        871
FT                   /note="I -> P (in Ref. 1; AAC51914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        929
FT                   /note="I -> F (in Ref. 1; AAC51914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1059
FT                   /note="K -> R (in Ref. 3; CAD38536)"
FT                   /evidence="ECO:0000305"
FT   HELIX           914..923
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          925..931
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           933..938
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           941..953
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          957..962
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          967..969
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           972..979
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           984..986
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          987..989
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           990..993
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           994..999
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          1001..1007
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           1010..1012
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           1015..1018
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   TURN            1023..1026
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           1032..1034
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          1035..1045
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           1055..1058
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   STRAND          1062..1067
FT                   /evidence="ECO:0007829|PDB:1DJL"
FT   HELIX           1069..1081
FT                   /evidence="ECO:0007829|PDB:1DJL"
SQ   SEQUENCE   1086 AA;  113896 MW;  8A437658CA0EB41B CRC64;
     MANLLKTVVT GCSCPLLSNL GSCKGLRVKK DFLRTFYTHQ ELWCKAPVKP GIPYKQLTVG
     VPKEIFQNEK RVALSPAGVQ NLVKQGFNVV VESGAGEASK FSDDHYRVAG AQIQGAKEVL
     ASDLVVKVRA PMVNPTLGVH EADLLKTSGT LISFIYPAQN PELLNKLSQR KTTVLAMDQV
     PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL
     ASAGAAKSMG AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE
     MKLFAQQCKE VDILISTALI PGKKAPVLFN KEMIESMKEG SVVVDLAAEA GGNFETTKPG
     ELYIHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFYFDV KDDFDFGTMG
     HVIRGTVVMK DGKVIFPAPT PKNIPQGAPV KQKTVAELEA EKAATITPFR KTMSTASAYT
     AGLTGILGLG IAAPNLAFSQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV
     GGLALMGGHL YPSTTSQGLA ALAAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
     PAGTFVGGYL AALYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA
     ATLGVLKPGP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCIA
     EYIIEYPHFA TDAAANLTKI VAYLGTYIGG VTFSGSLIAY GKLQGLLKSA PLLLPGRHLL
     NAGLLAASVG GIIPFMVDPS FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS
     YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG
     KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM LTEQGKKVRF
     GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT DLVLVIGAND TVNSAAQEDP
     NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV
     RESYQK
//