ALKBH_SCHPO
ID ALKBH_SCHPO Reviewed; 302 AA.
AC O60066; D3KZ45;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase abh1;
DE EC=1.14.11.-;
DE AltName: Full=Alkylated DNA repair protein alkB homolog;
GN Name=abh1; ORFNames=SPBC13G1.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-302.
RA Inatani S., Kanamitsu K., Ikeda S.;
RT "cDNA cloning of an AlkB homolog from Schizosaccharomyces pombe.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative dioxygenase that may repair alkylated DNA or RNA by
CC oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate
CC and iron (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; CU329671; CAA18657.3; -; Genomic_DNA.
DR EMBL; AB548892; BAI81891.1; -; mRNA.
DR PIR; T39405; T39405.
DR RefSeq; NP_596553.3; NM_001022474.3.
DR AlphaFoldDB; O60066; -.
DR SMR; O60066; -.
DR BioGRID; 276479; 8.
DR STRING; 4896.SPBC13G1.04c.1; -.
DR MaxQB; O60066; -.
DR PaxDb; O60066; -.
DR GeneID; 2539935; -.
DR KEGG; spo:SPBC13G1.04c; -.
DR PomBase; SPBC13G1.04c; abh1.
DR eggNOG; KOG2731; Eukaryota.
DR HOGENOM; CLU_029471_0_1_1; -.
DR InParanoid; O60066; -.
DR OMA; WHGVPKI; -.
DR PRO; PR:O60066; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990984; F:tRNA demethylase activity; ISS:PomBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:1990983; P:tRNA demethylation; ISS:PomBase.
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 2: Evidence at transcript level;
KW Dioxygenase; DNA damage; DNA repair; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..302
FT /note="Alpha-ketoglutarate-dependent dioxygenase abh1"
FT /id="PRO_0000066669"
FT DOMAIN 187..299
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 290..296
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 302 AA; 34348 MW; B4FD6B9D7618276C CRC64;
MLAGNMEQAN VFRLEEKRYK CRADTIPDMS EVLDPNDPQS FGFEALVEIK PRVFSFQKAP
GLLILKNYVS SELQMQLLKS IMFTQIQDPE NKTNLSPFYQ LPLGNDSIWR RYYNGDGESI
IDGLGETKPL TVDRLVHKKL RWVTLGEQYD WTTKEYPDPS KSPGFPKDLG DFVEKVVKES
TDFLHWKAEA AIVNFYSPGD TLSAHIDESE EDLTLPLISL SMGLDCIYLI GTESRSEKPS
ALRLHSGDVV IMTGTSRKAF HAVPKIIPNS TPNYLLTGNK AWDGWISRKR VNFNVRQVRP
SR
