ID BADH_SCHPO Reviewed; 500 AA. AC O59808; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 149. DE RecName: Full=Probable betaine aldehyde dehydrogenase; DE Short=BADH; DE EC=1.2.1.8; DE AltName: Full=Meiotic expression up-regulated protein 8; GN Name=meu8; ORFNames=SPCC550.10; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 420-500. RC STRAIN=CD16-1; RX PubMed=11376151; DOI=10.1093/nar/29.11.2327; RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y., RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.; RT "Comprehensive isolation of meiosis-specific genes identifies novel RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe."; RL Nucleic Acids Res. 29:2327-2337(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.8; CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via CC choline pathway; betaine from betaine aldehyde: step 1/1. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. 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; CU329672; CAA19114.1; -; Genomic_DNA. DR EMBL; AB054529; BAB60885.2; -; mRNA. DR PIR; T41385; T41385. DR RefSeq; NP_588102.1; NM_001023093.2. DR AlphaFoldDB; O59808; -. DR SMR; O59808; -. DR BioGRID; 275834; 7. DR STRING; 284812.O59808; -. DR PaxDb; 4896-SPCC550-10-1; -. DR EnsemblFungi; SPCC550.10.1; SPCC550.10.1:pep; SPCC550.10. DR GeneID; 2539264; -. DR KEGG; spo:SPCC550.10; -. DR PomBase; SPCC550.10; -. DR VEuPathDB; FungiDB:SPCC550.10; -. DR eggNOG; KOG2450; Eukaryota. DR HOGENOM; CLU_005391_0_2_1; -. DR InParanoid; O59808; -. DR OMA; GDHTSYV; -. DR PhylomeDB; O59808; -. DR UniPathway; UPA00529; UER00386. DR PRO; PR:O59808; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA:PomBase. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IC:PomBase. DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR CDD; cd07078; ALDH; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR PANTHER; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43860:SF2; BETAINE ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Meiosis; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..500 FT /note="Probable betaine aldehyde dehydrogenase" FT /id="PRO_0000056531" FT ACT_SITE 271 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT ACT_SITE 305 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT BINDING 249..254 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 173 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 500 AA; 54144 MW; BFFF9D7C1A11ACA0 CRC64; MTIDLNVIQS DIISARRAPE NSLFIDGKFV SPIEPAAKPI PLINPATEEI IGTCANASAK DVDSAVENAY NTFRSGIWAK WPGKQRGLVL RKIAKMMREK RELLAGIDTI NCGKPTPYAL FDIDSCADMF EYYAEVAETD NPTVKVPLPN NPGFCAFEKR FPRGVIGVIT PWNFPLKMAL WKLVPAIASG NCVVLKPSEL APWSCLEFAL ICKEAGLPDG VLNVIIGSGK ESGAALSCHP KIAYLAFTGS LATGKKIMHA AAENIVPLTL ELGGKSPLII CEDADLSLAI PSAAFAIFFN QGEACTAASR LIVHESVADE VLGGLVSEAN KLIIGNGLDP QVTLGPVVSK TQFEKIVSYI QSAINEGCKC VVGGLPRSEQ KGYFIPPTVF TNVQTHNKIW REEIFGPVLA VKTFHTNEEA LELANDSEYG LGSGVFSTNP KTLEFFSNNI EAGMCSLNNY HVVTHELPWI GWKHSGLGVG LSKHGYNEYM RLKQITQYVG //