We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback.
Take me to UniProt BETA
UniProtKB - P42412 (IOLA_BACSU)
Protein
Malonate-semialdehyde dehydrogenase
Gene
iolA
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively.
UniRule annotation3 PublicationsCatalytic activityi
- 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = H+ + hydrogencarbonate + NADH + propanoyl-CoAUniRule annotation2 PublicationsEC:1.2.1.27UniRule annotation2 Publications
Kineticsi
kcat is 7.4 sec(-1) with malonate semialdehyde as substrate. kcat is 1.1 sec(-1) with methylmalonate semialdehyde as substrate.1 Publication
- KM=0.12 mM for malonate semialdehyde (at 30 degrees Celsius and pH 8.2)1 Publication
- KM=0.06 mM for methylmalonate semialdehyde (at 30 degrees Celsius and pH 8.2)1 Publication
- KM=0.03 mM for CoA (with malonate semialdehyde at 30 degrees Celsius and pH 8.2)1 Publication
- KM=0.12 mM for CoA (with methylmalonate semialdehyde at 30 degrees Celsius and pH 8.2)1 Publication
- KM=1.78 mM for NAD (with malonate semialdehyde at 30 degrees Celsius and pH 8.2)1 Publication
- KM=2.3 mM for NAD (with methylmalonate semialdehyde at 30 degrees Celsius and pH 8.2)1 Publication
: myo-inositol degradation into acetyl-CoA Pathwayi
This protein is involved in step 7 of the subpathway that synthesizes acetyl-CoA from myo-inositol.UniRule annotation1 Publication This subpathway is part of the pathway myo-inositol degradation into acetyl-CoA, which is itself part of Polyol metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from myo-inositol, the pathway myo-inositol degradation into acetyl-CoA and in Polyol metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 284 | NucleophileUniRule annotationBy similarity | 1 | |
Binding sitei | 382 | NADUniRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 176 – 180 | NADUniRule annotation1 Publication | 5 |
GO - Molecular functioni
- malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity Source: RHEA
- malonate-semialdehyde dehydrogenase (acetylating) activity Source: GO_Central
- methylmalonate-semialdehyde dehydrogenase (acylating) activity Source: GO_Central
GO - Biological processi
- inositol catabolic process Source: UniProtKB-UniRule
- thymine catabolic process Source: GO_Central
- valine catabolic process Source: GO_Central
Keywordsi
Molecular function | Oxidoreductase |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | BSUB:BSU39760-MONOMER |
BRENDAi | 1.2.1.27, 658 |
SABIO-RKi | P42412 |
UniPathwayi | UPA00076;UER00148 |
Names & Taxonomyi
Protein namesi | Recommended name: Malonate-semialdehyde dehydrogenaseUniRule annotationCurated (EC:1.2.1.-2 Publications)Short name: MSA dehydrogenase1 PublicationUniRule annotation Alternative name(s): Methylmalonate-semialdehyde dehydrogenase1 PublicationUniRule annotation (EC:1.2.1.27UniRule annotation1 Publication) Short name: MMSA dehydrogenase1 PublicationUniRule annotation Short name: MMSDH Short name: MSDH1 PublicationUniRule annotation |
Gene namesi | Name:iolAUniRule annotation Synonyms:mmsA, yxdA Ordered Locus Names:BSU39760 ORF Names:E83A |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
No effect on vanillin degradation.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 36 | C → A: No effect at either the structural or enzymatic levels; when associated with A-160; A-287; A-351 and A-413. 1 Publication | 1 | |
Mutagenesisi | 107 | R → L: At least 50-fold decrease of the second-order rate constant for the acylation step. 1 Publication | 1 | |
Mutagenesisi | 160 | C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-287; A-351 and A-413. 1 Publication | 1 | |
Mutagenesisi | 283 | R → L: At least 50-fold decrease of the second-order rate constant for the acylation step. 1 Publication | 1 | |
Mutagenesisi | 287 | C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-351 and A-413. 1 Publication | 1 | |
Mutagenesisi | 351 | C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-413. 1 Publication | 1 | |
Mutagenesisi | 413 | C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056583 | 1 – 487 | Malonate-semialdehyde dehydrogenaseAdd BLAST | 487 |
Proteomic databases
jPOSTi | P42412 |
PaxDbi | P42412 |
Interactioni
Subunit structurei
Homotetramer.
UniRule annotation1 PublicationProtein-protein interaction databases
STRINGi | 224308.BSU39760 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P42412 |
SMRi | P42412 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P42412 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1012, Bacteria |
InParanoidi | P42412 |
OMAi | VGAAKEW |
PhylomeDBi | P42412 |
Family and domain databases
CDDi | cd07085, ALDH_F6_MMSDH, 1 hit |
Gene3Di | 3.40.309.10, 1 hit 3.40.605.10, 1 hit |
HAMAPi | MF_01670, IolA, 1 hit |
InterProi | View protein in InterPro IPR016161, Ald_DH/histidinol_DH IPR016163, Ald_DH_C IPR016160, Ald_DH_CS_CYS IPR016162, Ald_DH_N IPR015590, Aldehyde_DH_dom IPR010061, MeMal-semiAld_DH IPR023510, MSDH_GmP_bac |
PANTHERi | PTHR43866, PTHR43866, 1 hit |
Pfami | View protein in Pfam PF00171, Aldedh, 1 hit |
SUPFAMi | SSF53720, SSF53720, 1 hit |
TIGRFAMsi | TIGR01722, MMSDH, 1 hit |
PROSITEi | View protein in PROSITE PS00070, ALDEHYDE_DEHYDR_CYS, 1 hit |
i Sequence
Sequence statusi: Complete.
P42412-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAEIRKLKNY INGEWVESKT DQYEDVVNPA TKEVLCQVPI STKEDIDYAA
60 70 80 90 100
QTAAEAFKTW SKVAVPRRAR ILFNFQQLLS QHKEELAHLI TIENGKNTKE
110 120 130 140 150
ALGEVGRGIE NVEFAAGAPS LMMGDSLASI ATDVEAANYR YPIGVVGGIA
160 170 180 190 200
PFNFPMMVPC WMFPMAIALG NTFILKPSER TPLLTEKLVE LFEKAGLPKG
210 220 230 240 250
VFNVVYGAHD VVNGILEHPE IKAISFVGSK PVGEYVYKKG SENLKRVQSL
260 270 280 290 300
TGAKNHTIVL NDANLEDTVT NIVGAAFGSA GERCMACAVV TVEEGIADEF
310 320 330 340 350
MAKLQEKVAD IKIGNGLDDG VFLGPVIRED NKKRTLSYIE KGLEEGARLV
360 370 380 390 400
CDGRENVSDD GYFVGPTIFD NVTTEMTIWK DEIFAPVLSV IRVKNLKEAI
410 420 430 440 450
EIANKSEFAN GACLFTSNSN AIRYFRENID AGMLGINLGV PAPMAFFPFS
460 470 480
GWKSSFFGTL HANGKDSVDF YTRKKVVTAR YPAPDFN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB005554 Genomic DNA Translation: BAA21609.1 AL009126 Genomic DNA Translation: CAB16012.1 D14399 Genomic DNA Translation: BAA03290.1 |
PIRi | A69645 |
RefSeqi | NP_391855.1, NC_000964.3 WP_003243682.1, NZ_JNCM01000034.1 |
Genome annotation databases
EnsemblBacteriai | CAB16012; CAB16012; BSU_39760 |
GeneIDi | 937575 |
KEGGi | bsu:BSU39760 |
PATRICi | fig|224308.179.peg.4301 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB005554 Genomic DNA Translation: BAA21609.1 AL009126 Genomic DNA Translation: CAB16012.1 D14399 Genomic DNA Translation: BAA03290.1 |
PIRi | A69645 |
RefSeqi | NP_391855.1, NC_000964.3 WP_003243682.1, NZ_JNCM01000034.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1T90 | X-ray | 2.50 | A/B/C/D | 2-487 | [»] | |
AlphaFoldDBi | P42412 | |||||
SMRi | P42412 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU39760 |
Proteomic databases
jPOSTi | P42412 |
PaxDbi | P42412 |
Genome annotation databases
EnsemblBacteriai | CAB16012; CAB16012; BSU_39760 |
GeneIDi | 937575 |
KEGGi | bsu:BSU39760 |
PATRICi | fig|224308.179.peg.4301 |
Phylogenomic databases
eggNOGi | COG1012, Bacteria |
InParanoidi | P42412 |
OMAi | VGAAKEW |
PhylomeDBi | P42412 |
Enzyme and pathway databases
UniPathwayi | UPA00076;UER00148 |
BioCyci | BSUB:BSU39760-MONOMER |
BRENDAi | 1.2.1.27, 658 |
SABIO-RKi | P42412 |
Miscellaneous databases
EvolutionaryTracei | P42412 |
Family and domain databases
CDDi | cd07085, ALDH_F6_MMSDH, 1 hit |
Gene3Di | 3.40.309.10, 1 hit 3.40.605.10, 1 hit |
HAMAPi | MF_01670, IolA, 1 hit |
InterProi | View protein in InterPro IPR016161, Ald_DH/histidinol_DH IPR016163, Ald_DH_C IPR016160, Ald_DH_CS_CYS IPR016162, Ald_DH_N IPR015590, Aldehyde_DH_dom IPR010061, MeMal-semiAld_DH IPR023510, MSDH_GmP_bac |
PANTHERi | PTHR43866, PTHR43866, 1 hit |
Pfami | View protein in Pfam PF00171, Aldedh, 1 hit |
SUPFAMi | SSF53720, SSF53720, 1 hit |
TIGRFAMsi | TIGR01722, MMSDH, 1 hit |
PROSITEi | View protein in PROSITE PS00070, ALDEHYDE_DEHYDR_CYS, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | IOLA_BACSU | |
Accessioni | P42412Primary (citable) accession number: P42412 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | May 25, 2022 | |
This is version 161 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families