ID MMSA_BOVIN Reviewed; 537 AA. AC Q07536; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 16-JUN-2009, entry version 72. DE RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial; DE Short=MMSDH; DE Short=Malonate-semialdehyde dehydrogenase [acylating]; DE EC=1.2.1.27; DE EC=1.2.1.18; DE AltName: Full=Aldehyde dehydrogenase family 6 member A1; DE Flags: Precursor; GN Name=ALDH6A1; Synonyms=MMSDH; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX MEDLINE=93293905; PubMed=8514806; RA Deichaite I., Berthiaume L., Peseckis S.M., Patton W.F., Resh M.D.; RT "Novel use of an iodo-myristyl-CoA analog identifies a semialdehyde RT dehydrogenase in bovine liver."; RL J. Biol. Chem. 268:13738-13747(1993). CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds CC fatty acyl-CoA. CC -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O + CC NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. CC -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA CC + CO(2) + NAD(P)H. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L08643; AAA30650.1; -; mRNA. DR IPI; IPI00698279; -. DR PIR; A46600; A46600. DR RefSeq; NP_787005.1; -. DR UniGene; Bt.98765; -. DR HSSP; Q28399; 1O9J. DR Ensembl; ENSBTAG00000018469; Bos taurus. DR GeneID; 327692; -. DR KEGG; bta:327692; -. DR HOVERGEN; Q07536; -. DR BRENDA; 1.2.1.18; 251. DR BRENDA; 1.2.1.27; 251. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0000062; F:acyl-CoA binding; IDA:UniProtKB. DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetyl...; ISS:UniProtKB. DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (...; IDA:UniProtKB. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0019859; P:thymine metabolic process; ISS:UniProtKB. DR GO; GO:0006573; P:valine metabolic process; ISS:UniProtKB. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR010061; MeMal-semiAld_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR PANTHER; PTHR11699:SF27; MMSDH; 1. DR Pfam; PF00171; Aldedh; 1. DR TIGRFAMs; TIGR01722; MMSDH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG. PE 1: Evidence at protein level; KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; KW Oxidoreductase; Transit peptide. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 537 Methylmalonate-semialdehyde dehydrogenase FT [acylating], mitochondrial. FT /FTId=PRO_0000007188. FT NP_BIND 211 215 NAD (Potential). FT NP_BIND 263 268 NAD (Potential). FT ACT_SITE 319 319 Nucleophile (By similarity). FT BINDING 419 419 NAD (Potential). FT MOD_RES 57 57 N6-acetyllysine (By similarity). FT MOD_RES 119 119 N6-acetyllysine (By similarity). FT MOD_RES 333 333 N6-acetyllysine (By similarity). FT CONFLICT 126 127 ML -> TD (in Ref. 1; AA sequence). SQ SEQUENCE 537 AA; 58063 MW; 69DF39506E62F9C0 CRC64; MAAVAVAAAA AALRARILQV SSKVNSSWQP ASSFSSSSVP TVKLFIDGKF IESKSDKWID IHNPATNEVI GRVPESTKAE MDAAVSSCKR TFPAWADTSI LSRQQVLLRY QQLIKENLKE IARLIMLEQG KTLADAEGDV FRGLQVVEHA CSVTSLMLGD TMPSITKDMD LYSYRLPLGV CAGIAPFNFP AMIPLWMFPM AMVCGNTFLM KPSERVPGAT MLLAKLFQDS GAPDGTLNII HGQHEAVNFI CDHPDIKAIS FVGSNQAGEY IFERGSRHGK RVQANMGAKN HGVVMPDANK ENTLNQLVGA AFGAAGQRCM ALSTAILVGE AKKWLPELVE RAKKLRVNAG DQPGADLGPL ITPQAKERVC NLIDSGTKEG ASILLDGRSI KVKGYENGNF VGPTIISNVK PNMTCYKEEI FGPVLVVLET DTLDEAIKIV NDNPYGNGTA IFTTNGATAR KYSHLVDVGQ VGVNVPIPVP LPMFSFTGSR ASFRGDTNFY GKQGIQFYTQ LKTITSQWKE EDASLSSPAV VMPTMGR //