ID   IOLA2_BACSK             Reviewed;         486 AA.
AC   Q5WH11;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   29-MAY-2013, entry version 65.
DE   RecName: Full=Methylmalonate semialdehyde dehydrogenase [acylating] 2;
DE            Short=MMSA dehydrogenase 2;
DE            Short=MMSDH 2;
DE            Short=MSDH 2;
DE            EC=1.2.1.27;
DE   AltName: Full=Malonate semialdehyde dehydrogenase [acetylating] 2;
DE            Short=MSA dehydrogenase 2;
DE            EC=1.2.1.18;
GN   Name=iolA2; OrderedLocusNames=ABC1809;
OS   Bacillus clausii (strain KSM-K16).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii
RT   KSM-K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts malonate semialdehyde (MSA) and methylmalonate
CC       semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA,
CC       respectively (By similarity).
CC   -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA
CC       + CO(2) + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O +
CC       NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH.
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-
CC       CoA; acetyl-CoA from myo-inositol: step 7/7.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA
CC       subfamily.
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DR   EMBL; AP006627; BAD64344.1; -; Genomic_DNA.
DR   RefSeq; YP_175305.1; NC_006582.1.
DR   ProteinModelPortal; Q5WH11; -.
DR   SMR; Q5WH11; 5-484.
DR   STRING; 66692.ABC1809; -.
DR   EnsemblBacteria; BAD64344; BAD64344; ABC1809.
DR   GeneID; 3202963; -.
DR   KEGG; bcl:ABC1809; -.
DR   PATRIC; 18923124; VBIBacCla58185_1925.
DR   eggNOG; COG1012; -.
DR   HOGENOM; HOG000271507; -.
DR   KO; K00140; -.
DR   OMA; ELMCEAG; -.
DR   ProtClustDB; CLSK873284; -.
DR   BioCyc; BCLA66692:GHMP-1877-MONOMER; -.
DR   UniPathway; UPA00076; UER00148.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:HAMAP.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:HAMAP.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:HAMAP.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_01670; IolA; 1; -.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010061; MeMal-semiAld_DH.
DR   InterPro; IPR023510; MeMal-semiAld_DH_GmP_bac.
DR   PANTHER; PTHR11699:SF27; PTHR11699:SF27; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    486       Methylmalonate semialdehyde dehydrogenase
FT                                [acylating] 2.
FT                                /FTId=PRO_0000352327.
FT   NP_BIND     178    182       NAD (By similarity).
FT   ACT_SITE    286    286       Nucleophile (By similarity).
FT   BINDING     385    385       NAD (By similarity).
SQ   SEQUENCE   486 AA;  52752 MW;  DA534B62243E3144 CRC64;
     MTTTKVKTVK NWIDGAWVEA STADTEVVPN PATGEAIAYV PLSGERDVEQ AVASAKRAYE
     TWKTVPVPER TRYMFAYLEQ LKKNREQLAQ LITLENGKTI KDARGEVQRG IECVELATST
     PTMMMGDALP DIASGIDGSI WRYPLGVVAG ITPFNFPMMV PLWMFPLAIA AGNTFVLKTS
     ERTPLLAEQL VSLMHEVGLP RGVLNLVNGG KAVVNGLLNH PDVEAISFVG SEPVARYVYE
     TGTANGKRVQ ALAGAKNHAV VLADCELDKT VQGVIGAAFA SSGERCMACS VVAVVEEVAD
     AFIEKLTAET KKLTVGNGKN DEHFVGPLIR QSHKDKVVKY IEQGVEQGAE LLVDGRNATS
     EEAGYYLGAT LFDHVTPEMT IWQEELFAPV LSIVRVRDLE EAIALTNRSR FANGAVIYTS
     SGKAAQHFRN AIDAGMVGIN VNVPAPMAFF SFAGNKASFF GDLGTNGRDG IQFYTRKKVV
     TERWFN
//