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IOLA2_BACAH
ID   IOLA2_BACAH             Reviewed;         487 AA.
AC   A0REB5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Malonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01670};
DE   AltName: Full=Methylmalonate-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MMSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            Short=MSDH 2 {ECO:0000255|HAMAP-Rule:MF_01670};
DE            EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670};
GN   Name=iolA2 {ECO:0000255|HAMAP-Rule:MF_01670}; OrderedLocusNames=BALH_2259;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- FUNCTION: Catalyzes the oxidation of malonate semialdehyde (MSA) and
CC       methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA,
CC       respectively. {ECO:0000255|HAMAP-Rule:MF_01670}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH;
CC         Xref=Rhea:RHEA:22992, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000255|HAMAP-Rule:MF_01670};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC         hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01670};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK85558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000485; ABK85558.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000218120.1; NC_008600.1.
DR   AlphaFoldDB; A0REB5; -.
DR   SMR; A0REB5; -.
DR   EnsemblBacteria; ABK85558; ABK85558; BALH_2259.
DR   KEGG; btl:BALH_2259; -.
DR   HOGENOM; CLU_005391_1_10_9; -.
DR   UniPathway; UPA00076; UER00148.
DR   Proteomes; UP000000761; Chromosome.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
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; -; 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_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   NAD; Oxidoreductase.
FT   CHAIN           1..487
FT                   /note="Malonate-semialdehyde dehydrogenase 2"
FT                   /id="PRO_0000352334"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT   BINDING         178..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
FT   BINDING         386
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01670"
SQ   SEQUENCE   487 AA;  53127 MW;  AAB4168B3978860C CRC64;
     MTVQTAQIVK NYIGGEWVES ISTKMEAVYN PATGEVIAQV PLSTKGDVEQ AVLAANEAFK
     SWSKTAVPKR ARILFKYQQL LVDNWEELAK LITIENGKSY NEAYGEVLRG IECVEFAAGA
     PTLMMGKQLP DIATGIESGM YRYPIGVIGG ITPFNFPMMV PCWMFPLAIA CGNTFVLKPS
     ERTPLLAARL AELAEEAGLP KGVLNIVNGA HDVVNGLLEH KLVKAISFVG SQPVAEYVYK
     KGTENLKRVQ ALAGAKNHSI VLNDANLELA TKQIISAAFG SAGERCMAAS VVTVEEEIAD
     QLVERLVEEA NKIVIGNGLD EDVFLGPVIR DNHKERTIGY IDSGVEQGAT LVRDGREDTA
     VKGAGYFVGP TIFDHVTKEM KIWQDEIFAP VLSIVRVKSL DEAIEIANES RFANGACIYT
     DSGASVRQFR ETIESGMLGV NVGVPAPMAF FPFSGWKDSF YGDLHANGTD GVEFYTRKKM
     LTSRWEK
 
 
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