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Nucleic acid dioxygenase ALKBH1 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 1) (Alpha-ketoglutarate-dependent dioxygenase ABH1) (DNA 6mA demethylase) (DNA N6-methyl adenine demethylase) (EC 1.14.11.-) (DNA lyase ABH1) (EC 4.2.99.18) (DNA oxidative demethylase ALKBH1) (EC 1.14.11.33) (tRNA N1-methyl adenine demethylase) (EC 1.14.11.-)

 ALKB1_HUMAN             Reviewed;         389 AA.
Q13686; Q8TAU1; Q9ULA7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
27-SEP-2017, entry version 142.
RecName: Full=Nucleic acid dioxygenase ALKBH1 {ECO:0000305};
EC=1.14.11.- {ECO:0000269|PubMed:27497299};
AltName: Full=Alkylated DNA repair protein alkB homolog 1 {ECO:0000303|PubMed:19959401};
AltName: Full=Alpha-ketoglutarate-dependent dioxygenase ABH1 {ECO:0000303|PubMed:19959401};
AltName: Full=DNA 6mA demethylase {ECO:0000250|UniProtKB:P0CB42};
AltName: Full=DNA N6-methyl adenine demethylase {ECO:0000250|UniProtKB:P0CB42};
EC=1.14.11.- {ECO:0000250|UniProtKB:P0CB42};
AltName: Full=DNA lyase ABH1 {ECO:0000303|PubMed:19959401};
EC=4.2.99.18 {ECO:0000305|PubMed:19959401};
AltName: Full=DNA oxidative demethylase ALKBH1;
EC=1.14.11.33 {ECO:0000305|PubMed:18603530};
AltName: Full=tRNA N1-methyl adenine demethylase {ECO:0000305|PubMed:27745969};
EC=1.14.11.- {ECO:0000269|PubMed:27745969};
Name=ALKBH1 {ECO:0000312|HGNC:HGNC:17911};
Synonyms=ABH {ECO:0000303|PubMed:17979886},
ABH1 {ECO:0000303|PubMed:19959401}, ALKBH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Synovial sarcoma;
PubMed=8600462; DOI=10.1093/nar/24.5.931;
Wei Y.F., Carter K.C., Wang R.P., Shell B.K.;
"Molecular cloning and functional analysis of a human cDNA encoding an
Escherichia coli AlkB homolog, a protein involved in DNA alkylation
damage repair.";
Nucleic Acids Res. 24:931-937(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17979886; DOI=10.1111/j.1582-4934.2007.00094.x;
Tsujikawa K., Koike K., Kitae K., Shinkawa A., Arima H., Suzuki T.,
Tsuchiya M., Makino Y., Furukawa T., Konishi N., Yamamoto H.;
"Expression and sub-cellular localization of human ABH family
molecules.";
J. Cell. Mol. Med. 11:1105-1116(2007).
[5]
FUNCTION, COFACTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-218;
HIS-231; ASP-233; HIS-287; ARG-338 AND ARG-344, IDENTIFICATION BY MASS
SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=18603530; DOI=10.1074/jbc.M803776200;
Westbye M.P., Feyzi E., Aas P.A., Vagbo C.B., Talstad V.A., Kavli B.,
Hagen L., Sundheim O., Akbari M., Liabakk N.B., Slupphaug G.,
Otterlei M., Krokan H.E.;
"Human AlkB homolog 1 is a mitochondrial protein that demethylates 3-
methylcytosine in DNA and RNA.";
J. Biol. Chem. 283:25046-25056(2008).
[6]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-231; ASP-233 AND HIS-287.
PubMed=19959401; DOI=10.1016/j.dnarep.2009.10.011;
Muller T.A., Meek K., Hausinger R.P.;
"Human AlkB homologue 1 (ABH1) exhibits DNA lyase activity at abasic
sites.";
DNA Repair 9:58-65(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[8]
SUBCELLULAR LOCATION.
PubMed=22961808; DOI=10.1002/stem.1228;
Ougland R., Lando D., Jonson I., Dahl J.A., Moen M.N.,
Nordstrand L.M., Rognes T., Lee J.T., Klungland A., Kouzarides T.,
Larsen E.;
"ALKBH1 is a histone H2A dioxygenase involved in neural
differentiation.";
Stem Cells 30:2672-2682(2012).
[9]
FUNCTION, AND MUTAGENESIS OF LYS-3; LYS-25; LYS-55; LYS-61; LYS-64;
LYS-87; LYS-94; LYS-116; LYS-120; LYS-125; LYS-133; LYS-137; LYS-148;
LYS-154; LYS-158; LYS-167; LYS-182; LYS-183; LYS-241; LYS-335; LYS-362
AND LYS-381.
PubMed=23577621; DOI=10.1042/BJ20121908;
Mueller T.A., Andrzejak M.M., Hausinger R.P.;
"A covalent protein-DNA 5'-product adduct is generated following AP
lyase activity of human ALKBH1 (AlkB homologue 1).";
Biochem. J. 452:509-518(2013).
[10]
MUTAGENESIS OF HIS-113; CYS-118; CYS-129; HIS-134; HIS-303; CYS-304;
CYS-371 AND HIS-372.
PubMed=25459764; DOI=10.1016/j.jmgm.2014.10.013;
Silvestrov P., Mueller T.A., Clark K.N., Hausinger R.P.,
Cisneros G.A.;
"Homology modeling, molecular dynamics, and site-directed mutagenesis
study of AlkB human homolog 1 (ALKBH1).";
J. Mol. Graph. Model. 54:123-130(2014).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 231-HIS--ASP-233.
PubMed=27745969; DOI=10.1016/j.cell.2016.09.038;
Liu F., Clark W., Luo G., Wang X., Fu Y., Wei J., Wang X., Hao Z.,
Dai Q., Zheng G., Ma H., Han D., Evans M., Klungland A., Pan T.,
He C.;
"ALKBH1-mediated tRNA demethylation regulates translation.";
Cell 167:816-828(2016).
[12]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-233 AND ARG-338.
PubMed=27497299; DOI=10.15252/embj.201694885;
Haag S., Sloan K.E., Ranjan N., Warda A.S., Kretschmer J.,
Blessing C., Huebner B., Seikowski J., Dennerlein S., Rehling P.,
Rodnina M.V., Hoebartner C., Bohnsack M.T.;
"NSUN3 and ABH1 modify the wobble position of mt-tRNAMet to expand
codon recognition in mitochondrial translation.";
EMBO J. 35:2104-2119(2016).
-!- FUNCTION: Dioxygenase that acts as on nucleic acids, such as DNA
and tRNA (PubMed:18603530, PubMed:27745969, PubMed:27497299).
Requires molecular oxygen, alpha-ketoglutarate and iron
(PubMed:18603530, PubMed:27497299). A number of activities have
been described for this dioxygenase, but recent results suggest
that it mainly acts as on tRNAs and mediates their demethylation
or oxidation depending on the context and subcellular compartment
(PubMed:27745969, PubMed:27497299). Mainly acts as a tRNA
demethylase by removing N(1)-methyladenine from various tRNAs,
with a preference for N(1)-methyladenine at position 58 (m1A58)
present on a stem loop structure of tRNAs (PubMed:27745969). Acts
as a regulator of translation initiation and elongation in
response to glucose deprivation: regulates both translation
initiation, by mediating demethylation of tRNA(Met), and
translation elongation, N(1)-methyladenine-containing tRNAs being
preferentially recruited to polysomes to promote translation
elongation (PubMed:27745969). In mitochondrion, specifically
interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met)
methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at
this position (PubMed:27497299). mt-tRNA(Met) containing the f(5)c
modification at the wobble position enables recognition of the AUA
codon in addition to the AUG codon, expanding codon recognition in
mitochondrial translation (PubMed:27497299). Specifically
demethylates DNA methylated on the 6th position of adenine (N(6)-
methyladenosine) DNA. N(6)-methyladenosine (m6A) DNA is present at
some L1 elements in embryonic stem cells and probably promotes
their silencing (By similarity). Also able to repair alkylated
single-stranded DNA and RNA containing 3-methylcytosine by
oxidative demethylation, but with low activity (PubMed:18603530).
Also has DNA lyase activity and introduces double-stranded breaks
at abasic sites: cleaves both single-stranded DNA and double-
stranded DNA at abasic sites, with the greatest activity towards
double-stranded DNA with two abasic sites (PubMed:19959401). DNA
lyase activity does not require alpha-ketboglutarate and iron and
leads to the formation of an irreversible covalent protein-DNA
adduct with the 5' DNA product (PubMed:19959401, PubMed:23577621).
DNA lyase activity is not required during base excision repair and
class switch recombination of the immunoglobulin heavy chain
during B lymphocyte activation. May play a role in placental
trophoblast lineage differentiation (By similarity).
{ECO:0000250|UniProtKB:P0CB42, ECO:0000269|PubMed:18603530,
ECO:0000269|PubMed:19959401, ECO:0000269|PubMed:23577621,
ECO:0000269|PubMed:27497299, ECO:0000269|PubMed:27745969}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000305|PubMed:19959401}.
-!- CATALYTIC ACTIVITY: DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA-
base + formaldehyde + succinate + CO(2).
{ECO:0000305|PubMed:18603530}.
-!- CATALYTIC ACTIVITY: N(6)-methyladenine in DNA + 2-oxoglutarate +
O(2) = adenine in DNA + formaldehyde + succinate + CO(2).
{ECO:0000250|UniProtKB:P0CB42}.
-!- CATALYTIC ACTIVITY: N(1)-methyladenine in tRNA + 2-oxoglutarate +
O(2) = adenine in tRNA + formaldehyde + succinate + CO(2).
{ECO:0000269|PubMed:27745969}.
-!- CATALYTIC ACTIVITY: 5-methylcytosine(34) in mitochondrial
tRNA(Met)+ 2-oxoglutarate + O(2) = 5-formylcytosine(34) in
mitochondrial tRNA(Met) + formaldehyde + succinate + CO(2).
{ECO:0000269|PubMed:27497299}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:18603530};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00805};
-!- SUBUNIT: Monomer (PubMed:19959401). Interacts with DNAJB6 (By
similarity). {ECO:0000250|UniProtKB:P0CB42,
ECO:0000269|PubMed:19959401}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22961808}.
Mitochondrion {ECO:0000269|PubMed:17979886,
ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:27497299}.
Note=Mainly localizes in euchromatin, largely excluded from
heterochromatin and nucleoli (By similarity).
{ECO:0000250|UniProtKB:P0CB42}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17979886,
ECO:0000269|PubMed:18603530}.
-!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
-!- CAUTION: The DNA N6-methyl adenine demethylase activity is unclear
in vivo. According to a recent report, biochemical assays do not
reveal clear DNA N6-methyl adenine demethylase activity in vivo.
{ECO:0000269|PubMed:27745969}.
-!- SEQUENCE CAUTION:
Sequence=CAA63047.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; X91992; CAA63047.1; ALT_FRAME; mRNA.
EMBL; AC008044; AAF01478.1; -; Genomic_DNA.
EMBL; BC025787; AAH25787.1; -; mRNA.
CCDS; CCDS32127.1; -.
PIR; S64736; S64736.
RefSeq; NP_006011.2; NM_006020.2.
UniGene; Hs.94542; -.
ProteinModelPortal; Q13686; -.
BioGrid; 114372; 2.
IntAct; Q13686; 1.
STRING; 9606.ENSP00000216489; -.
iPTMnet; Q13686; -.
PhosphoSitePlus; Q13686; -.
BioMuta; ALKBH1; -.
EPD; Q13686; -.
MaxQB; Q13686; -.
PaxDb; Q13686; -.
PeptideAtlas; Q13686; -.
PRIDE; Q13686; -.
DNASU; 8846; -.
Ensembl; ENST00000216489; ENSP00000216489; ENSG00000100601.
GeneID; 8846; -.
KEGG; hsa:8846; -.
UCSC; uc001xuc.2; human.
CTD; 8846; -.
DisGeNET; 8846; -.
EuPathDB; HostDB:ENSG00000100601.9; -.
GeneCards; ALKBH1; -.
H-InvDB; HIX0011855; -.
HGNC; HGNC:17911; ALKBH1.
HPA; HPA044087; -.
MIM; 605345; gene.
neXtProt; NX_Q13686; -.
OpenTargets; ENSG00000100601; -.
PharmGKB; PA134906996; -.
eggNOG; KOG2731; Eukaryota.
eggNOG; COG3145; LUCA.
GeneTree; ENSGT00390000004599; -.
HOGENOM; HOG000033905; -.
HOVERGEN; HBG050487; -.
InParanoid; Q13686; -.
KO; K10765; -.
OMA; CYHAVPR; -.
OrthoDB; EOG091G0A10; -.
PhylomeDB; Q13686; -.
TreeFam; TF314609; -.
ChiTaRS; ALKBH1; human.
GenomeRNAi; 8846; -.
PRO; PR:Q13686; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100601; -.
CleanEx; HS_ALKBH1; -.
ExpressionAtlas; Q13686; baseline and differential.
Genevisible; Q13686; HS.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; IBA:GO_Central.
GO; GO:0103053; F:1-ethyladenine demethylase activity; IEA:UniProtKB-EC.
GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IBA:GO_Central.
GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
GO; GO:0070579; F:methylcytosine dioxygenase activity; IDA:UniProtKB.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO; GO:1990984; F:tRNA demethylase activity; IDA:UniProtKB.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:UniProtKB.
GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0070989; P:oxidative demethylation; IDA:UniProtKB.
GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IBA:GO_Central.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0070129; P:regulation of mitochondrial translation; IMP:UniProtKB.
GO; GO:0006448; P:regulation of translational elongation; IMP:UniProtKB.
GO; GO:0006446; P:regulation of translational initiation; IMP:UniProtKB.
GO; GO:0042245; P:RNA repair; IDA:UniProtKB.
GO; GO:1990983; P:tRNA demethylation; IDA:UniProtKB.
GO; GO:0002101; P:tRNA wobble cytosine modification; IDA:UniProtKB.
Gene3D; 2.60.120.590; -; 1.
InterPro; IPR004574; Alkb.
InterPro; IPR027450; AlkB-like.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
PANTHER; PTHR16557; PTHR16557; 1.
Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
TIGRFAMs; TIGR00568; alkb; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
Complete proteome; Dioxygenase; DNA damage; DNA repair; Iron; Lyase;
Metal-binding; Mitochondrion; Multifunctional enzyme; Nucleus;
Oxidoreductase; Polymorphism; Reference proteome; RNA repair;
Translation regulation.
CHAIN 1 389 Nucleic acid dioxygenase ALKBH1.
/FTId=PRO_0000066668.
DOMAIN 208 347 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
REGION 86 389 tRNA-binding.
{ECO:0000305|PubMed:27745969}.
REGION 175 177 Substrate binding.
{ECO:0000250|UniProtKB:Q6NS38}.
REGION 220 222 Alpha-ketoglutarate binding.
{ECO:0000250|UniProtKB:Q96Q83}.
REGION 338 344 Alpha-ketoglutarate binding.
{ECO:0000250|UniProtKB:Q96Q83}.
METAL 231 231 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805,
ECO:0000305|PubMed:19959401,
ECO:0000305|PubMed:27745969}.
METAL 233 233 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805,
ECO:0000305|PubMed:19959401,
ECO:0000305|PubMed:27497299,
ECO:0000305|PubMed:27745969}.
METAL 287 287 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
BINDING 144 144 Substrate.
{ECO:0000250|UniProtKB:Q6NS38}.
BINDING 233 233 Substrate.
{ECO:0000250|UniProtKB:Q6NS38}.
SITE 133 133 Primary catalytic residue forming the
imine linkage with DNA.
{ECO:0000269|PubMed:23577621}.
SITE 133 133 Secondary catalytic residue forming the
imine linkage with DNA.
{ECO:0000269|PubMed:23577621}.
VARIANT 135 135 M -> I (in dbSNP:rs17825440).
/FTId=VAR_048221.
VARIANT 324 324 M -> L (in dbSNP:rs6494).
/FTId=VAR_048222.
MUTAGEN 3 3 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 25 25 K->A: Moderate decrease in DNA lyase
activity. Reduced DNA lyase activity;
when associated with A-133.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 55 55 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 61 61 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 64 64 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 87 87 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 94 94 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 113 113 H->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 116 116 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 118 118 C->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 120 120 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 125 125 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 129 129 C->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 133 133 K->A: Reduced DNA lyase activity.
Slightly more reduced DNA lyase activity;
when associated with A-25. Strongly
reduced activity; when associated with A-
154. {ECO:0000269|PubMed:23577621}.
MUTAGEN 134 134 H->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 137 137 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 148 148 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 154 154 K->A: Does not affect DNA lyase activity.
Strongly reduced activity; when
associated with A-133.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 158 158 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 167 167 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 182 182 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 183 183 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 218 218 I->L: Reduces Fe2OG dioxygenase activity
by 50%. {ECO:0000269|PubMed:18603530}.
MUTAGEN 231 233 HVD->AVA: Loss of catalytic activity.
Abolishes ability to regulate translation
in respose to glucose deprivation.
{ECO:0000269|PubMed:27745969}.
MUTAGEN 231 231 H->A: Near loss of Fe2OG dioxygenase
activity. No effect on DNA lyase
activity. {ECO:0000269|PubMed:18603530,
ECO:0000269|PubMed:19959401}.
MUTAGEN 233 233 D->A: Loss of Fe2OG dioxygenase activity.
No effect on DNA lyase activity.
Abolishes ability to mediate oxidation of
mt-tRNA(Met) methylated at cytosine(34)
to form 5-formylcytosine (f(5)c).
{ECO:0000269|PubMed:18603530,
ECO:0000269|PubMed:19959401,
ECO:0000269|PubMed:27497299}.
MUTAGEN 241 241 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 287 287 H->A: Loss of Fe2OG dioxygenase activity.
No effect on DNA lyase activity.
{ECO:0000269|PubMed:18603530,
ECO:0000269|PubMed:19959401}.
MUTAGEN 303 303 H->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 304 304 C->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 335 335 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 338 338 R->A: Reduced Fe2OG dioxygenase activity.
Abolishes ability to mediate oxidation of
mt-tRNA(Met) methylated at cytosine(34)
to form 5-formylcytosine (f(5)c).
{ECO:0000269|PubMed:18603530,
ECO:0000269|PubMed:27497299}.
MUTAGEN 344 344 R->A: Reduced Fe2OG dioxygenase activity.
{ECO:0000269|PubMed:18603530}.
MUTAGEN 362 362 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
MUTAGEN 371 371 C->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 372 372 H->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:25459764}.
MUTAGEN 381 381 K->A: Does not affect DNA lyase activity.
{ECO:0000269|PubMed:23577621}.
CONFLICT 133 133 K -> T (in Ref. 1; CAA63047).
{ECO:0000305}.
CONFLICT 266 267 TA -> PP (in Ref. 1; CAA63047).
{ECO:0000305}.
CONFLICT 388 388 D -> H (in Ref. 3; AAH25787).
{ECO:0000305}.
SEQUENCE 389 AA; 43832 MW; 539C4CE41D2D8AEC CRC64;
MGKMAAAVGS VATLATEPGE DAFRKLFRFY RQSRPGTADL EGVIDFSAAH AARGKGPGAQ
KVIKSQLNVS SVSEQNAYRA GLQPVSKWQA YGLKGYPGFI FIPNPFLPGY QWHWVKQCLK
LYSQKPNVCN LDKHMSKEET QDLWEQSKEF LRYKEATKRR PRSLLEKLRW VTVGYHYNWD
SKKYSADHYT PFPSDLGFLS EQVAAACGFE DFRAEAGILN YYRLDSTLGI HVDRSELDHS
KPLLSFSFGQ SAIFLLGGLQ RDEAPTAMFM HSGDIMIMSG FSRLLNHAVP RVLPNPEGEG
LPHCLEAPLP AVLPRDSMVE PCSMEDWQVC ASYLKTARVN MTVRQVLATD QNFPLEPIED
EKRDISTEGF CHLDDQNSEV KRARINPDS


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