YKN3_SCHPO
ID YKN3_SCHPO Reviewed; 407 AA.
AC Q9HDX2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=FMN-dependent alpha-hydroxy acid dehydrogenase PB1A11.03 {ECO:0000305};
DE EC=1.13.12.- {ECO:0000305};
GN ORFNames=SPAPB1A11.03;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00683};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAC19728.1; -; Genomic_DNA.
DR RefSeq; NP_593999.1; NM_001019425.2.
DR AlphaFoldDB; Q9HDX2; -.
DR SMR; Q9HDX2; -.
DR BioGRID; 279823; 2.
DR STRING; 4896.SPAPB1A11.03.1; -.
DR iPTMnet; Q9HDX2; -.
DR MaxQB; Q9HDX2; -.
DR PaxDb; Q9HDX2; -.
DR EnsemblFungi; SPAPB1A11.03.1; SPAPB1A11.03.1:pep; SPAPB1A11.03.
DR GeneID; 2543401; -.
DR KEGG; spo:SPAPB1A11.03; -.
DR PomBase; SPAPB1A11.03; -.
DR VEuPathDB; FungiDB:SPAPB1A11.03; -.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_0_1_1; -.
DR InParanoid; Q9HDX2; -.
DR OMA; FDSGIRC; -.
DR PhylomeDB; Q9HDX2; -.
DR Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SPO-390918; Peroxisomal lipid metabolism.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
DR PRO; PR:Q9HDX2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; ISO:PomBase.
DR GO; GO:0050040; F:lactate 2-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR GO; GO:0006089; P:lactate metabolic process; ISO:PomBase.
DR CDD; cd03332; LMO_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR037350; LMO_FMN.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Flavoprotein; FMN; Monooxygenase; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..407
FT /note="FMN-dependent alpha-hydroxy acid dehydrogenase
FT PB1A11.03"
FT /id="PRO_0000316582"
FT DOMAIN 28..406
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 54
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 160
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 197
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 277
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 304
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 332..336
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 355..356
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
SQ SEQUENCE 407 AA; 45311 MW; B0039309D1093CA4 CRC64;
MFRNYNWFDA KEPISYESEI YAKGLKFQRP QITVDGRHWE QLAVERMTKD AAGYVYGCAG
KRETYDKNME SFKKWSIIPN RLIKSGFPDL STTVFGQKYP FPIALAPVGV QKIFNPEGES
GSCAAATREH IPYIISTASA TSFEDIEKAS GPGERWYQLY WPSNDHQDIT ISLLNRAKKT
GCRVLIVTLD TFILGWRPSD MDNGYDPFLN PDSIGVEHGF SDPVFRKQFK EKHGVEVEEN
MLEAAKEFAG IVFPGISHDW EDLKFLRKHW DGPIVLKGIM NVPDAKKAVE YGMQGIVVSN
HGGRQQDGGV ASLTMLPKIV DAVGDKLDVL FDSGVRSGAD IAKALALGAK MVLIGRPYVY
GLALEGSSGV SHVIRCLLGD LELTLHLSGI VSVKPKDLNR DVLYKEE
