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Database: UniProt
Entry: A0A0D1Y9K1_ANEMI
LinkDB: A0A0D1Y9K1_ANEMI
Original site: A0A0D1Y9K1_ANEMI 
ID   A0A0D1Y9K1_ANEMI        Unreviewed;       487 AA.
AC   A0A0D1Y9K1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-FEB-2018, entry version 26.
DE   RecName: Full=Malonate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE            Short=MSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.- {ECO:0000256|HAMAP-Rule:MF_01670};
DE   AltName: Full=Methylmalonate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE            Short=MMSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01670};
DE            Short=MSDH {ECO:0000256|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.27 {ECO:0000256|HAMAP-Rule:MF_01670};
GN   Name=iolA {ECO:0000256|HAMAP-Rule:MF_01670};
GN   ORFNames=AF333_08925 {ECO:0000313|EMBL:KON95572.1}, SAMN04487909_10311
GN   {ECO:0000313|EMBL:SDI30436.1};
OS   Aneurinibacillus migulanus (Bacillus migulanus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=47500 {ECO:0000313|EMBL:KON95572.1, ECO:0000313|Proteomes:UP000037269};
RN   [1] {ECO:0000313|EMBL:KON95572.1, ECO:0000313|Proteomes:UP000037269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:KON95572.1,
RC   ECO:0000313|Proteomes:UP000037269};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Fjat-14205 dsm 2895.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SDI30436.1, ECO:0000313|Proteomes:UP000182836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:SDI30436.1,
RC   ECO:0000313|Proteomes:UP000182836};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|HAMAP-Rule:MF_01670}.
CC   -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O +
CC       NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. {ECO:0000256|HAMAP-
CC       Rule:MF_01670}.
CC   -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(+) = acetyl-CoA +
CC       CO(2) + NADH. {ECO:0000256|HAMAP-Rule:MF_01670}.
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-
CC       CoA; acetyl-CoA from myo-inositol: step 7/7. {ECO:0000256|HAMAP-
CC       Rule:MF_01670}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01670}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01670}.
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DR   EMBL; LGUG01000004; KON95572.1; -; Genomic_DNA.
DR   EMBL; FNED01000003; SDI30436.1; -; Genomic_DNA.
DR   RefSeq; WP_043066162.1; NZ_LGUG01000004.1.
DR   EnsemblBacteria; KON95572; KON95572; AF333_08925.
DR   PATRIC; fig|47500.8.peg.7091; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000037269; Unassembled WGS sequence.
DR   Proteomes; UP000182836; Unassembled WGS sequence.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
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 {ECO:0000313|Proteomes:UP000037269,
KW   ECO:0000313|Proteomes:UP000182836};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01670};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037269}.
FT   DOMAIN       19    481       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   NP_BIND     180    184       NAD. {ECO:0000256|HAMAP-Rule:MF_01670}.
FT   ACT_SITE    288    288       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01670}.
FT   BINDING     388    388       NAD. {ECO:0000256|HAMAP-Rule:MF_01670}.
SQ   SEQUENCE   487 AA;  53115 MW;  E58989BA045A3634 CRC64;
     MTLAKDKVQH VKNFVGGVWV ESTAERYEEV PNPATGETIA YVPISSREEL DRAVAVAKEA
     YKTWKKVAVP RRARILFKYQ QLLVEHWDEL ARLITIENGK SYEEAYGEVQ RGIECVEFAA
     GAPTLMMGTQ LPDIATGVES GMYRYPIGVV GGITPFNFPM MVPCWMFPLA IACGNTFVLK
     PSERTPLLAN RLAELFTEAG LPEGVLNVVH GAHDVVNGIL ENQDVKAVSF VGSQPVAEYV
     YKTAAANGKR VQALAGAKNH SIVMPDADLD NAVKNIIGAA FGSAGERCMA CAVVVAVGDI
     ADELVHRLTV EAEQIKIGNG LDEGVFLGPV IRDSHKARTI GYIEAGEKEG ARLVRDGRTD
     QAANGEGYFV GPTIFDNVTT EMSIWKDEIF APVLSVVRVK DLDEAIELTN QSEFANGACL
     YTDSAKAVRQ FRDDIDAGML GINLGVPAPM AFFPFSGYKK SFYGDLHANG RDGVEFYTRK
     KMLTARY
//
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