IOLA_BACSU
ID IOLA_BACSU Reviewed; 487 AA.
AC P42412;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Malonate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000305};
DE Short=MSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000303|PubMed:18310071};
DE EC=1.2.1.- {ECO:0000269|PubMed:16332250, ECO:0000269|PubMed:18310071};
DE AltName: Full=Methylmalonate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000303|PubMed:16332250};
DE Short=MMSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000303|PubMed:16332250};
DE Short=MMSDH;
DE Short=MSDH {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000303|PubMed:16332250};
DE EC=1.2.1.27 {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000269|PubMed:16332250};
GN Name=iolA {ECO:0000255|HAMAP-Rule:MF_01670}; Synonyms=mmsA, yxdA;
GN OrderedLocusNames=BSU39760; ORFNames=E83A;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT between the gnt and iol operons.";
RL DNA Res. 2:61-69(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-487.
RC STRAIN=168 / BGSC1A1;
RX PubMed=7952181; DOI=10.1099/13500872-140-9-2289;
RA Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
RT "Cloning and nucleotide sequencing of a 15 kb region of the Bacillus
RT subtilis genome containing the iol operon.";
RL Microbiology 140:2289-2298(1994).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, MUTAGENESIS OF CYS-36;
RP CYS-160; CYS-287; CYS-351 AND CYS-413, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16332250; DOI=10.1042/bj20051525;
RA Stines-Chaumeil C., Talfournier F., Branlant G.;
RT "Mechanistic characterization of the MSDH (methylmalonate semialdehyde
RT dehydrogenase) from Bacillus subtilis.";
RL Biochem. J. 395:107-115(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=168 / 60015;
RX PubMed=18310071; DOI=10.1074/jbc.m708043200;
RA Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H.,
RA Fujita Y.;
RT "Myo-inositol catabolism in Bacillus subtilis.";
RL J. Biol. Chem. 283:10415-10424(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, AND MUTAGENESIS OF
RP ARG-107 AND ARG-283.
RX PubMed=21515690; DOI=10.1074/jbc.m110.213280;
RA Talfournier F., Stines-Chaumeil C., Branlant G.;
RT "Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis:
RT substrate specificity and coenzyme A binding.";
RL J. Biol. Chem. 286:21971-21981(2011).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / 3NA;
RX PubMed=26658822; DOI=10.1007/s00253-015-7197-6;
RA Graf N., Wenzel M., Altenbuchner J.;
RT "Identification and characterization of the vanillin dehydrogenase YfmT in
RT Bacillus subtilis 3NA.";
RL Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-487 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=15272169; DOI=10.1107/s0907444904012533;
RA Dubourg H., Stines-Chaumeil C., Didierjean C., Talfournier F.,
RA Rahuel-Clermont S., Branlant G., Aubry A.;
RT "Expression, purification, crystallization and preliminary X-ray
RT diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus
RT subtilis.";
RL Acta Crystallogr. D 60:1435-1437(2004).
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 ECO:0000269|PubMed:16332250, ECO:0000269|PubMed:18310071,
CC ECO:0000269|PubMed:21515690}.
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 ECO:0000269|PubMed:16332250, ECO:0000269|PubMed:18310071};
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 ECO:0000269|PubMed:16332250, ECO:0000269|PubMed:21515690};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for malonate semialdehyde (at 30 degrees Celsius and pH
CC 8.2) {ECO:0000269|PubMed:16332250};
CC KM=0.06 mM for methylmalonate semialdehyde (at 30 degrees Celsius and
CC pH 8.2) {ECO:0000269|PubMed:16332250};
CC KM=0.03 mM for CoA (with malonate semialdehyde at 30 degrees Celsius
CC and pH 8.2) {ECO:0000269|PubMed:16332250};
CC KM=0.12 mM for CoA (with methylmalonate semialdehyde at 30 degrees
CC Celsius and pH 8.2) {ECO:0000269|PubMed:16332250};
CC KM=1.78 mM for NAD (with malonate semialdehyde at 30 degrees Celsius
CC and pH 8.2) {ECO:0000269|PubMed:16332250};
CC KM=2.3 mM for NAD (with methylmalonate semialdehyde at 30 degrees
CC Celsius and pH 8.2) {ECO:0000269|PubMed:16332250};
CC Note=kcat is 7.4 sec(-1) with malonate semialdehyde as substrate.
CC kcat is 1.1 sec(-1) with methylmalonate semialdehyde as substrate.
CC {ECO:0000269|PubMed:16332250};
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, ECO:0000269|PubMed:18310071}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01670,
CC ECO:0000269|PubMed:15272169}.
CC -!- DISRUPTION PHENOTYPE: No effect on vanillin degradation.
CC {ECO:0000269|PubMed:26658822}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01670, ECO:0000305}.
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DR EMBL; AB005554; BAA21609.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16012.1; -; Genomic_DNA.
DR EMBL; D14399; BAA03290.1; -; Genomic_DNA.
DR PIR; A69645; A69645.
DR RefSeq; NP_391855.1; NC_000964.3.
DR RefSeq; WP_003243682.1; NZ_JNCM01000034.1.
DR PDB; 1T90; X-ray; 2.50 A; A/B/C/D=2-487.
DR PDBsum; 1T90; -.
DR AlphaFoldDB; P42412; -.
DR SMR; P42412; -.
DR STRING; 224308.BSU39760; -.
DR jPOST; P42412; -.
DR PaxDb; P42412; -.
DR PRIDE; P42412; -.
DR EnsemblBacteria; CAB16012; CAB16012; BSU_39760.
DR GeneID; 937575; -.
DR KEGG; bsu:BSU39760; -.
DR PATRIC; fig|224308.179.peg.4301; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P42412; -.
DR OMA; VGAAKEW; -.
DR PhylomeDB; P42412; -.
DR BioCyc; BSUB:BSU39760-MON; -.
DR BioCyc; MetaCyc:BSU39760-MON; -.
DR BRENDA; 1.2.1.27; 658.
DR SABIO-RK; P42412; -.
DR UniPathway; UPA00076; UER00148.
DR EvolutionaryTrace; P42412; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IBA:GO_Central.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..487
FT /note="Malonate-semialdehyde dehydrogenase"
FT /id="PRO_0000056583"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25526, ECO:0000255|HAMAP-
FT Rule:MF_01670"
FT BINDING 176..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670,
FT ECO:0000269|PubMed:15272169"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01670,
FT ECO:0000269|PubMed:15272169"
FT MUTAGEN 36
FT /note="C->A: No effect at either the structural or
FT enzymatic levels; when associated with A-160; A-287; A-351
FT and A-413."
FT /evidence="ECO:0000269|PubMed:16332250"
FT MUTAGEN 107
FT /note="R->L: At least 50-fold decrease of the second-order
FT rate constant for the acylation step."
FT /evidence="ECO:0000269|PubMed:21515690"
FT MUTAGEN 160
FT /note="C->A: No effect at either the structural or
FT enzymatic levels; when associated with A-36; A-287; A-351
FT and A-413."
FT /evidence="ECO:0000269|PubMed:16332250"
FT MUTAGEN 283
FT /note="R->L: At least 50-fold decrease of the second-order
FT rate constant for the acylation step."
FT /evidence="ECO:0000269|PubMed:21515690"
FT MUTAGEN 287
FT /note="C->A: No effect at either the structural or
FT enzymatic levels; when associated with A-36; A-160; A-351
FT and A-413."
FT /evidence="ECO:0000269|PubMed:16332250"
FT MUTAGEN 351
FT /note="C->A: No effect at either the structural or
FT enzymatic levels; when associated with A-36; A-160; A-287
FT and A-413."
FT /evidence="ECO:0000269|PubMed:16332250"
FT MUTAGEN 413
FT /note="C->A: No effect at either the structural or
FT enzymatic levels; when associated with A-36; A-160; A-287
FT and A-351."
FT /evidence="ECO:0000269|PubMed:16332250"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1T90"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 385..395
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:1T90"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:1T90"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:1T90"
SQ SEQUENCE 487 AA; 53453 MW; 412B63B05869229F CRC64;
MAEIRKLKNY INGEWVESKT DQYEDVVNPA TKEVLCQVPI STKEDIDYAA QTAAEAFKTW
SKVAVPRRAR ILFNFQQLLS QHKEELAHLI TIENGKNTKE ALGEVGRGIE NVEFAAGAPS
LMMGDSLASI ATDVEAANYR YPIGVVGGIA PFNFPMMVPC WMFPMAIALG NTFILKPSER
TPLLTEKLVE LFEKAGLPKG VFNVVYGAHD VVNGILEHPE IKAISFVGSK PVGEYVYKKG
SENLKRVQSL TGAKNHTIVL NDANLEDTVT NIVGAAFGSA GERCMACAVV TVEEGIADEF
MAKLQEKVAD IKIGNGLDDG VFLGPVIRED NKKRTLSYIE KGLEEGARLV CDGRENVSDD
GYFVGPTIFD NVTTEMTIWK DEIFAPVLSV IRVKNLKEAI EIANKSEFAN GACLFTSNSN
AIRYFRENID AGMLGINLGV PAPMAFFPFS GWKSSFFGTL HANGKDSVDF YTRKKVVTAR
YPAPDFN
