ALKB1_MOUSE
ID ALKB1_MOUSE Reviewed; 389 AA.
AC P0CB42;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nucleic acid dioxygenase ALKBH1 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000305|PubMed:27027282};
DE AltName: Full=Alkylated DNA repair protein alkB homolog 1;
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase ABH1 {ECO:0000250|UniProtKB:Q13686};
DE AltName: Full=DNA 6mA demethylase {ECO:0000305|PubMed:27027282};
DE AltName: Full=DNA N6-methyl adenine demethylase ALKBH1 {ECO:0000305|PubMed:27027282};
DE EC=1.14.11.51 {ECO:0000305|PubMed:27027282};
DE AltName: Full=DNA lyase ABH1 {ECO:0000250|UniProtKB:Q13686};
DE EC=4.2.99.18 {ECO:0000250|UniProtKB:Q13686};
DE AltName: Full=DNA oxidative demethylase ALKBH1;
DE EC=1.14.11.33 {ECO:0000250|UniProtKB:Q13686};
DE AltName: Full=mRNA N(3)-methylcytidine demethylase {ECO:0000305};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:Q13686};
DE AltName: Full=tRNA N1-methyl adenine demethylase {ECO:0000250|UniProtKB:Q13686};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:Q13686};
GN Name=Alkbh1 {ECO:0000312|MGI:MGI:2384034};
GN Synonyms=Abh {ECO:0000250|UniProtKB:Q13686}, Alkbh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION, INTERACTION WITH DNAJB6, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18163532; DOI=10.1002/dvdy.21418;
RA Pan Z., Sikandar S., Witherspoon M., Dizon D., Nguyen T., Benirschke K.,
RA Wiley C., Vrana P., Lipkin S.M.;
RT "Impaired placental trophoblast lineage differentiation in Alkbh1(-/-)
RT mice.";
RL Dev. Dyn. 237:316-327(2008).
RN [3]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=21072209; DOI=10.1371/journal.pone.0013827;
RA Nordstrand L.M., Svaerd J., Larsen E., Nilsen A., Ougland R., Furu K.,
RA Lien G.F., Rognes T., Namekawa S.H., Lee J.T., Klungland A.;
RT "Mice lacking Alkbh1 display sex-ratio distortion and unilateral eye
RT defects.";
RL PLoS ONE 5:E13827-E13827(2010).
RN [4]
RP POSSIBLE FUNCTION AS A HISTONE DEMETHYLASE.
RX PubMed=22961808; DOI=10.1002/stem.1228;
RA Ougland R., Lando D., Jonson I., Dahl J.A., Moen M.N., Nordstrand L.M.,
RA Rognes T., Lee J.T., Klungland A., Kouzarides T., Larsen E.;
RT "ALKBH1 is a histone H2A dioxygenase involved in neural differentiation.";
RL Stem Cells 30:2672-2682(2012).
RN [5]
RP FUNCTION.
RX PubMed=23825659; DOI=10.1371/journal.pone.0067403;
RA Mueller T.A., Yu K., Hausinger R.P., Meek K.;
RT "ALKBH1 is dispensable for abasic site cleavage during base excision repair
RT and class switch recombination.";
RL PLoS ONE 8:E67403-E67403(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-233.
RX PubMed=27027282; DOI=10.1038/nature17640;
RA Wu T.P., Wang T., Seetin M.G., Lai Y., Zhu S., Lin K., Liu Y., Byrum S.D.,
RA Mackintosh S.G., Zhong M., Tackett A., Wang G., Hon L.S., Fang G.,
RA Swenberg J.A., Xiao A.Z.;
RT "DNA methylation on N(6)-adenine in mammalian embryonic stem cells.";
RL Nature 532:329-333(2016).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27745969; DOI=10.1016/j.cell.2016.09.038;
RA Liu F., Clark W., Luo G., Wang X., Fu Y., Wei J., Wang X., Hao Z., Dai Q.,
RA Zheng G., Ma H., Han D., Evans M., Klungland A., Pan T., He C.;
RT "ALKBH1-mediated tRNA demethylation regulates translation.";
RL Cell 167:816-828(2016).
CC -!- FUNCTION: Dioxygenase that acts as on nucleic acids, such as DNA and
CC tRNA (PubMed:27027282, PubMed:27745969). Requires molecular oxygen,
CC alpha-ketoglutarate and iron (PubMed:27027282). A number of activities
CC have been described for this dioxygenase, but recent results suggest
CC that it mainly acts as on tRNAs and mediates their demethylation or
CC oxidation depending on the context and subcellular compartment (By
CC similarity). Mainly acts as a tRNA demethylase by removing N(1)-
CC methyladenine from various tRNAs, with a preference for N(1)-
CC methyladenine at position 58 (m1A58) present on a stem loop structure
CC of tRNAs (PubMed:27745969). Acts as a regulator of translation
CC initiation and elongation in response to glucose deprivation: regulates
CC both translation initiation, by mediating demethylation of tRNA(Met),
CC and translation elongation, N(1)-methyladenine-containing tRNAs being
CC preferentially recruited to polysomes to promote translation elongation
CC (By similarity). In mitochondrion, specifically interacts with mt-
CC tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at
CC cytosine(34) to form 5-formylcytosine (f(5)c) at this position (By
CC similarity). mt-tRNA(Met) containing the f(5)c modification at the
CC wobble position enables recognition of the AUA codon in addition to the
CC AUG codon, expanding codon recognition in mitochondrial translation (By
CC similarity). Specifically demethylates DNA methylated on the 6th
CC position of adenine (N(6)-methyladenosine) DNA (PubMed:27027282). N(6)-
CC methyladenosine (m6A) DNA is present at some L1 elements in embryonic
CC stem cells and probably promotes their silencing (PubMed:27027282).
CC Demethylates mRNAs containing N(3)-methylcytidine modification (By
CC similarity). Also able to repair alkylated single-stranded DNA by
CC oxidative demethylation, but with low activity (By similarity). Also
CC has DNA lyase activity and introduces double-stranded breaks at abasic
CC sites: cleaves both single-stranded DNA and double-stranded DNA at
CC abasic sites, with the greatest activity towards double-stranded DNA
CC with two abasic sites (By similarity). DNA lyase activity does not
CC require alpha-ketboglutarate and iron and leads to the formation of an
CC irreversible covalent protein-DNA adduct with the 5' DNA product (By
CC similarity). DNA lyase activity is not required during base excision
CC repair and class switch recombination of the immunoglobulin heavy chain
CC during B lymphocyte activation (PubMed:23825659). May play a role in
CC placental trophoblast lineage differentiation (PubMed:18163532).
CC {ECO:0000250|UniProtKB:Q13686, ECO:0000269|PubMed:18163532,
CC ECO:0000269|PubMed:23825659, ECO:0000269|PubMed:27027282,
CC ECO:0000269|PubMed:27745969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2
CC = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:49524, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:90616; EC=1.14.11.51;
CC Evidence={ECO:0000305|PubMed:27027282};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC Evidence={ECO:0000250|UniProtKB:Q13686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a
CC nucleobase within DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:32875,
CC ChEBI:CHEBI:64428; EC=1.14.11.33;
CC Evidence={ECO:0000250|UniProtKB:Q13686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(1)-methyladenosine in tRNA + O2 = an
CC adenosine in tRNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:54576, Rhea:RHEA-COMP:10242, Rhea:RHEA-COMP:12312,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74491; Evidence={ECO:0000250|UniProtKB:Q13686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + 5-methylcytidine(34) in mitochondrial
CC tRNA(Met) + 2 O2 = 5-formylcytidine(34) in mitochondrial tRNA(Met) +
CC 2 CO2 + H2O + 2 succinate; Xref=Rhea:RHEA:54144, Rhea:RHEA-
CC COMP:13808, Rhea:RHEA-COMP:13809, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:74483, ChEBI:CHEBI:138075;
CC Evidence={ECO:0000250|UniProtKB:Q13686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(3)-methylcytidine in mRNA + O2 = a
CC cytidine in mRNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:60920, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15713,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74894,
CC ChEBI:CHEBI:82748; Evidence={ECO:0000250|UniProtKB:Q13686};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60921;
CC Evidence={ECO:0000250|UniProtKB:Q13686};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:27027282};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with DNAJB6
CC (PubMed:18163532). {ECO:0000250|UniProtKB:Q13686,
CC ECO:0000269|PubMed:18163532}.
CC -!- INTERACTION:
CC P0CB42; O54946-2: Dnajb6; NbExp=2; IntAct=EBI-13941048, EBI-13941040;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18163532}.
CC Note=Mainly localizes in euchromatin, largely excluded from
CC heterochromatin and nucleoli. {ECO:0000269|PubMed:18163532}.
CC -!- TISSUE SPECIFICITY: In adult organs, highly expressed in testis, eye,
CC brain and kidney. {ECO:0000269|PubMed:21072209}.
CC -!- DEVELOPMENTAL STAGE: Weak expression throughout the embryo at 8.5 dpc.
CC As the cells migrate and differentiate during organogenesis, expressed
CC in the spinal cord, forebrain and branchial arches at 9.5 dpc, and also
CC in limb buds at 10.5 dpc. Peak expression at 11.5 dpc in the
CC frontonasal process including telencephalon, maxillary, mandibular and
CC hyoid arches, upper and lower limb buds and midbrain and rhombomere 1
CC roof plates. Expression decreases considerably from 11.5 dpc to 12.5
CC dpc (PubMed:21072209). At 8.5 dpc is highly expressed in the chorion
CC and the ectoplacental cone. At 10.5 dpc is highly expressed in multiple
CC trophoblast lineages (spongiotrophoblasts, giant cell trophoblasts,
CC glycogen cells, and labyrinthine trophoblasts). The highest placental
CC level is at 9.5 dpc and subsequently decreases until parturition
CC (PubMed:18163532). {ECO:0000269|PubMed:18163532,
CC ECO:0000269|PubMed:21072209}.
CC -!- DISRUPTION PHENOTYPE: Deficiency results in 80% reduction of the litter
CC size due to embryonic lethality (PubMed:21072209, PubMed:23825659).
CC Surviving pups exhibit a gender bias in favor of males (70% males and
CC 30% females) (PubMed:21072209, PubMed:23825659). Intrauterine growth
CC retardation and placental defects. Altered expression of trophoblast
CC lineage-specific genes (PubMed:18163532). Increased N(6)-
CC methyladenosine (m6A) DNA (PubMed:27027282). No effect on H2AK118 or
CC H2AK119 methylation, suggesting that Alkbh1 does not act as a histone
CC demethylase in vivo (PubMed:27027282). Cells show an strong increase of
CC N(1)-methyladenine-containing tRNAs (PubMed:27745969).
CC {ECO:0000269|PubMed:18163532, ECO:0000269|PubMed:21072209,
CC ECO:0000269|PubMed:27027282, ECO:0000269|PubMed:27745969}.
CC -!- CAUTION: H2A histone demethylase activity was observed in vitro
CC (PubMed:22961808). The relevance of such activity is however unclear
CC and additional experimental evidence would be needed to confirm this
CC activity in vivo. {ECO:0000269|PubMed:22961808}.
CC -!- CAUTION: The DNA N6-methyl adenine demethylase activity is subject to
CC discussion. While DNA N6-methyl adenine demethylase activity was
CC observed by a report (PubMed:27027282). Another group was unable to
CC detect clear DNA N6-methyl adenine demethylase activity in vivo
CC (PubMed:27745969). {ECO:0000269|PubMed:27027282,
CC ECO:0000269|PubMed:27745969}.
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DR EMBL; CT030249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49120.1; -.
DR RefSeq; NP_001096035.1; NM_001102565.1.
DR PDB; 6IMA; X-ray; 2.59 A; A/B/C=37-369.
DR PDB; 6IMC; X-ray; 2.51 A; A/B/C/D=1-359.
DR PDB; 6KSF; X-ray; 2.40 A; A=20-355.
DR PDB; 6L94; X-ray; 3.10 A; A=4-389.
DR PDBsum; 6IMA; -.
DR PDBsum; 6IMC; -.
DR PDBsum; 6KSF; -.
DR PDBsum; 6L94; -.
DR AlphaFoldDB; P0CB42; -.
DR SMR; P0CB42; -.
DR IntAct; P0CB42; 1.
DR STRING; 10090.ENSMUSP00000124565; -.
DR iPTMnet; P0CB42; -.
DR PhosphoSitePlus; P0CB42; -.
DR EPD; P0CB42; -.
DR jPOST; P0CB42; -.
DR MaxQB; P0CB42; -.
DR PaxDb; P0CB42; -.
DR PRIDE; P0CB42; -.
DR ProteomicsDB; 296396; -.
DR Antibodypedia; 26095; 264 antibodies from 31 providers.
DR Ensembl; ENSMUST00000162961; ENSMUSP00000124565; ENSMUSG00000079036.
DR GeneID; 211064; -.
DR KEGG; mmu:211064; -.
DR UCSC; uc007oix.1; mouse.
DR CTD; 8846; -.
DR MGI; MGI:2384034; Alkbh1.
DR VEuPathDB; HostDB:ENSMUSG00000079036; -.
DR eggNOG; KOG2731; Eukaryota.
DR GeneTree; ENSGT00390000004599; -.
DR HOGENOM; CLU_029471_2_1_1; -.
DR InParanoid; P0CB42; -.
DR OMA; WDTKKYS; -.
DR OrthoDB; 1045321at2759; -.
DR PhylomeDB; P0CB42; -.
DR TreeFam; TF314609; -.
DR BRENDA; 1.14.11.51; 3474.
DR BioGRID-ORCS; 211064; 3 hits in 110 CRISPR screens.
DR ChiTaRS; Alkbh1; mouse.
DR PRO; PR:P0CB42; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P0CB42; protein.
DR Bgee; ENSMUSG00000079036; Expressed in humerus cartilage element and 231 other tissues.
DR ExpressionAtlas; P0CB42; baseline and differential.
DR Genevisible; P0CB42; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; IDA:MGI.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0070579; F:methylcytosine dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IDA:UniProtKB.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:1990984; F:tRNA demethylase activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB.
DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0070989; P:oxidative demethylation; ISS:UniProtKB.
DR GO; GO:0035513; P:oxidative RNA demethylation; ISS:UniProtKB.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IBA:GO_Central.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0070129; P:regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0006448; P:regulation of translational elongation; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0042245; P:RNA repair; ISS:UniProtKB.
DR GO; GO:1990983; P:tRNA demethylation; IMP:UniProtKB.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; ISS:UniProtKB.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR004574; Alkb.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR16557; PTHR16557; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR TIGRFAMs; TIGR00568; alkb; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; DNA damage; DNA repair; Iron; Lyase;
KW Metal-binding; Multifunctional enzyme; Nucleus; Oxidoreductase;
KW Reference proteome; RNA repair; Translation regulation.
FT CHAIN 1..389
FT /note="Nucleic acid dioxygenase ALKBH1"
FT /id="PRO_0000386453"
FT DOMAIN 213..347
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..127
FT /note="Interaction with DNAJB6"
FT /evidence="ECO:0000269|PubMed:18163532"
FT REGION 86..389
FT /note="tRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13686"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 220..222
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96Q83"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000305|PubMed:27027282"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 338..344
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96Q83"
FT MUTAGEN 233
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27027282"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6IMC"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6KSF"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6KSF"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:6KSF"
FT TURN 153..157
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6IMA"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:6KSF"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:6KSF"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:6KSF"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:6KSF"
SQ SEQUENCE 389 AA; 43746 MW; D18C019F0CB9C0A5 CRC64;
MGKMAAAVAS LATLAAEPRE DAFRKLFRFY RQSRPGTADL GAVIDFSEAH LARSPKPGVP
QVVRFPLNVS SVTERDAERV GLEPVSKWRA YGLEGYPGFI FIPNPFLPGC QRHWVKQCLK
LYSQKPNVCN LDKHMTKEET QGLWEQSKEV LRSKEVTKRR PRSLLERLRW VTLGYHYNWD
SKKYSADHYT PFPSDLAFLS EQVATACGFQ GFQAEAGILN YYRLDSTLGI HVDRSELDHS
KPLLSFSFGQ SAIFLLGGLK RDEAPTAMFM HSGDIMVMSG FSRLLNHAVP RVLPHPDGEC
LPHCLETPLP AVLPSNSLVE PCSVEDWQVC ATYLRTARVN MTVRQVLATG QDFPLEPVEE
TKRDIAADGL CHLHDPNSPV KRKRLNPNS
