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Database: UniProt
Entry: IOLA1_BACSK
LinkDB: IOLA1_BACSK
Original site: IOLA1_BACSK 
ID   IOLA1_BACSK             Reviewed;         491 AA.
AC   Q5WKZ1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   28-FEB-2018, entry version 94.
DE   RecName: Full=Malonate-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01670};
DE   AltName: Full=Methylmalonate-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MMSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSDH 1 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA1 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   OrderedLocusNames=ABC0422;
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: Catalyzes the oxidation of malonate semialdehyde (MSA)
CC       and methylmalonate semialdehyde (MMSA) into acetyl-CoA and
CC       propanoyl-CoA, respectively. {ECO:0000255|HAMAP-Rule:MF_01670}.
CC   -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(+) = acetyl-CoA +
CC       CO(2) + NADH. {ECO:0000255|HAMAP-Rule:MF_01670}.
CC   -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O +
CC       NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. {ECO:0000255|HAMAP-
CC       Rule:MF_01670}.
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-
CC       CoA; acetyl-CoA from myo-inositol: step 7/7. {ECO:0000255|HAMAP-
CC       Rule:MF_01670}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01670}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01670}.
DR   EMBL; AP006627; BAD62964.1; -; Genomic_DNA.
DR   RefSeq; WP_011245283.1; NC_006582.1.
DR   ProteinModelPortal; Q5WKZ1; -.
DR   SMR; Q5WKZ1; -.
DR   STRING; 66692.ABC0422; -.
DR   EnsemblBacteria; BAD62964; BAD62964; ABC0422.
DR   GeneID; 34045067; -.
DR   KEGG; bcl:ABC0422; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271507; -.
DR   KO; K00140; -.
DR   OMA; SQWKEED; -.
DR   OrthoDB; POG091H0B1P; -.
DR   BioCyc; BCLA66692:G1G25-464-MONOMER; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:UniProtKB-EC.
DR   CDD; cd07085; ALDH_F6_MMSDH; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
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_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010061; MeMal-semiAld_DH.
DR   InterPro; IPR023510; MSDH_GmP_bac.
DR   PANTHER; PTHR43866; PTHR43866; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    491       Malonate-semialdehyde dehydrogenase 1.
FT                                /FTId=PRO_0000352326.
FT   NP_BIND     180    184       NAD. {ECO:0000255|HAMAP-Rule:MF_01670}.
FT   ACT_SITE    288    288       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01670}.
FT   BINDING     386    386       NAD. {ECO:0000255|HAMAP-Rule:MF_01670}.
SQ   SEQUENCE   491 AA;  53477 MW;  D12D2FFD4698A92B CRC64;
     MGETTVEVRK VKNYINGKWI ESSTSLYEDV VNPATKEVIC QVPLSTKADV EYAVEAAKTA
     FAKWSKVAVP RRARILFNYQ QLLQRDKEEL ARLITIENGK NLTEARGEVQ RGIENVEFAA
     GAPSLMMGDS LPMIATDVEA SNYRYPIGVV GGIAPFNFPM MVPCWMFPMA IALGNAFLLK
     PSERTPLLTE KLADLLTEAG VPDGVFNVVY GAHDVVNGML EHPDIKAISF VGSKPVGEYV
     YKKASENLKR VQALTGAKNH TIVLNDADLD DAVTNIAGAA FGSAGERCMA CAVVTVEEGI
     ADAFVAKLKA KAESLVMGNG LDDGVFLGPV IREENKNRTI AYIEKGVEEG ATLVCDGRSR
     VSADGYFIGP TIFENVTTDM TIWKDEIFAP VLSIIRVKNL DEGIQIANRS EFANGACLFT
     TNAAAVRYFR ENIDAGMLGI NLGVPAPMAF FPFSGWKSSF YGTLHANGKD SVDFYTRKKV
     VTARYPKPSF D
//
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