ALKB6_XENLA
ID ALKB6_XENLA Reviewed; 240 AA.
AC Q5PQ59;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
DE EC=1.14.11.-;
DE AltName: Full=Alkylated DNA repair protein alkB homolog 6;
GN Name=alkbh6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable dioxygenase that requires molecular oxygen, alpha-
CC ketoglutarate and iron. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; BC087349; AAH87349.1; -; mRNA.
DR RefSeq; NP_001088709.1; NM_001095240.1.
DR RefSeq; XP_018084621.1; XM_018229132.1.
DR AlphaFoldDB; Q5PQ59; -.
DR SMR; Q5PQ59; -.
DR DNASU; 495973; -.
DR GeneID; 495973; -.
DR KEGG; xla:495973; -.
DR CTD; 495973; -.
DR Xenbase; XB-GENE-5891959; alkbh6.L.
DR OrthoDB; 1573279at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 495973; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032862; ALKBH6.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR46030; PTHR46030; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..240
FT /note="Alpha-ketoglutarate-dependent dioxygenase alkB
FT homolog 6"
FT /id="PRO_0000323719"
FT DOMAIN 95..227
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 102..104
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 218..224
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 27077 MW; 045F2D1CF573951E CRC64;
MQACHNFPDL DSFLVEKIPL AAYYVPEYIS KSEEEYLLRQ VYNAPKPKWT QLSGRKLQNW
GGLPHSRGMV QEKLPSWLQK YTDQISSLGV FGDHSANHVL VNEYNAGEGI MPHEDGPMYY
PTVTTISLGS HTLLDFYVPI NKECQETQNQ DKVASTEEQR HMLSLLLEPR SLLVVREELY
TSYLHGICPR TSDTLSPMVA NLGNSTAHAG DTLQRGTRVS LTIRFVPKVL KTSLLLGKGR