Reviewed, UniProtKB/Swiss-Prot P42412 (IOLA_BACSU)

Names and origin

Protein names

Recommended name:
    Methylmalonate semialdehyde dehydrogenase [acylating]
      Short name=MMSA dehydrogenase
      Short name=MMSDH
      Short name=MSDH
    EC=1.2.1.27
Alternative name(s):
    Malonate semialdehyde dehydrogenase [acetylating]
      Short name=MSA dehydrogenase
    EC=1.2.1.18

Gene names

Name:	iolA
Synonyms:	mmsA, yxdA
Ordered Locus Names:	BSU39760
ORF Names:	E83A

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. Ref.4 Ref.5
Catalytic activity	3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H. Ref.4 Ref.5 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH. Ref.4 Ref.5
Pathway	Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7. HAMAP MF_01670
Subunit structure	Homotetramer. Ref.6
Sequence similarities	Belongs to the aldehyde dehydrogenase family. IolA subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.03 mM for CoA (with malonate semialdehyde at 30 degrees Celsius and pH 8.2) HAMAP MF_01670 KM=0.6 mM for methylmalonate semialdehyde (at 30 degrees Celsius and pH 8.2) KM=0.12 mM for CoA (with methylmalonate semialdehyde at 30 degrees Celsius and pH 8.2) KM=0.12 mM for malonate semialdehyde (at 30 degrees Celsius and pH 8.2) KM=1.78 mM for NAD (with malonate semialdehyde at 30 degrees Celsius and pH 8.2) KM=2.3 mM for NAD (with methylmalonate semialdehyde at 30 degrees Celsius and pH 8.2)

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	inositol catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW valine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	malonate-semialdehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: HAMAP methylmalonate-semialdehyde dehydrogenase (acylating) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 487

487

Methylmalonate semialdehyde dehydrogenase [acylating] HAMAP MF_01670

PRO_0000056583

Regions

Nucleotide binding

176 – 180

5

NAD HAMAP MF_01670

Sites

Active site

284

1

Nucleophile HAMAP MF_01670

Binding site

382

1

NAD HAMAP MF_01670

Experimental info

Mutagenesis

36

1

C → A: No effect at either the structural or enzymatic levels; when associated with A-160; A-287; A-351 and A-413. Ref.4

Mutagenesis

160

1

C → A: No effect at either the structural or enzymatic levels when associated with A-36; A-287, A-351 and A-413. Ref.4

Mutagenesis

287

1

C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-351 and A-413. Ref.4

Mutagenesis

351

1

C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-413. Ref.4

Mutagenesis

413

1

C → A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351. Ref.4

Secondary structure

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487

Helix Strand Turn

Details...

Beta strand

9 – 11

3

Beta strand

14 – 16

3

Beta strand

23 – 27

5

Turn

29 – 31

3

Beta strand

34 – 39

6

Helix

43 – 60

18

Helix

65 – 80

16

Helix

83 – 94

12

Helix

98 – 115

18

Helix

118 – 122

5

Beta strand

124 – 131

8

Beta strand

134 – 142

9

Beta strand

144 – 149

6

Helix

157 – 168

12

Beta strand

172 – 176

5

Beta strand

179 – 181

3

Helix

183 – 194

12

Beta strand

201 – 204

4

Helix

209 – 217

9

Beta strand

221 – 228

8

Helix

230 – 242

13

Beta strand

246 – 250

5

Beta strand

255 – 259

5

Helix

265 – 277

13

Helix

278 – 281

4

Beta strand

287 – 293

7

Helix

294 – 308

15

Helix

329 – 344

16

Beta strand

348 – 351

4

Beta strand

353 – 356

4

Beta strand

359 – 362

4

Beta strand

367 – 371

5

Helix

377 – 380

4

Beta strand

385 – 395

11

Helix

396 – 405

10

Beta strand

406 – 415

10

Helix

419 – 428

10

Beta strand

432 – 437

6

Beta strand

456 – 460

5

Helix

464 – 470

7

Beta strand

472 – 480

9

Sequences

	Sequence		Length	Mass (Da)
	P42412-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 412B63B05869229F	FASTA	487	53,453
	10 20 30 40 50 60 MAEIRKLKNY INGEWVESKT DQYEDVVNPA TKEVLCQVPI STKEDIDYAA QTAAEAFKTW 70 80 90 100 110 120 SKVAVPRRAR ILFNFQQLLS QHKEELAHLI TIENGKNTKE ALGEVGRGIE NVEFAAGAPS 130 140 150 160 170 180 LMMGDSLASI ATDVEAANYR YPIGVVGGIA PFNFPMMVPC WMFPMAIALG NTFILKPSER 190 200 210 220 230 240 TPLLTEKLVE LFEKAGLPKG VFNVVYGAHD VVNGILEHPE IKAISFVGSK PVGEYVYKKG 250 260 270 280 290 300 SENLKRVQSL TGAKNHTIVL NDANLEDTVT NIVGAAFGSA GERCMACAVV TVEEGIADEF 310 320 330 340 350 360 MAKLQEKVAD IKIGNGLDDG VFLGPVIRED NKKRTLSYIE KGLEEGARLV CDGRENVSDD 370 380 390 400 410 420 GYFVGPTIFD NVTTEMTIWK DEIFAPVLSV IRVKNLKEAI EIANKSEFAN GACLFTSNSN 430 440 450 460 470 480 AIRYFRENID AGMLGINLGV PAPMAFFPFS GWKSSFFGTL HANGKDSVDF YTRKKVVTAR YPAPDFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons." Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y. DNA Res. 2:61-69(1995) [PubMed: 7584049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon." Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y. Microbiology 140:2289-2298(1994) [PubMed: 7952181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-487. Strain: 168 / BGSC1A1.
[4]	"Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis." Stines-Chaumeil C., Talfournier F., Branlant G. Biochem. J. 395:107-115(2006) [PubMed: 16332250] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, MUTAGENESIS OF CYS-36; CYS-160; CYS-287; CYS-351 AND CYS-413, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Myo-inositol catabolism in Bacillus subtilis." Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H., Fujita Y. J. Biol. Chem. 283:10415-10424(2008) [PubMed: 18310071] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: 168 / 60015.
[6]	"Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis." Dubourg H., Stines-Chaumeil C., Didierjean C., Talfournier F., Rahuel-Clermont S., Branlant G., Aubry A. Acta Crystallogr. D 60:1435-1437(2004) [PubMed: 15272169] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-487 IN COMPLEX WITH NAD, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB005554 Genomic DNA. Translation: BAA21609.1.
AL009126 Genomic DNA. Translation: CAB16012.1.
D14399 Genomic DNA. Translation: BAA03290.1.

PIR

A69645.

RefSeq

NP_391855.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T90	X-ray	2.50	A/B/C/D	2-487	[»]

ModBase

Search...

Genome annotation databases

GeneID

937575.

GenomeReviews

Gene locus BSU39760 in contig AL009126_GR.

KEGG

bsu:BSU39760.

NMPDR

fig|224308.1.peg.3981.

Organism-specific databases

SubtiList

BG11117. iolA. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P42412.

OMA

P42412. DARAWIP.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU3972-MON.

BRENDA

1.2.1.27. 150.

Family and domain databases

HAMAP

MF_01670.
[Tree]

InterPro

IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR010061. MeMal-semiAld_DH.
[Graphical view]

Gene3D

G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.

PANTHER

PTHR11699. Aldehyde_dehyd. 1 hit.
PTHR11699:SF27. MMSDH. 1 hit.

Pfam

PF00171. Aldedh. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01722. MMSDH. 1 hit.

PROSITE

PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

IOLA_BACSU

Accession

Primary (citable) accession number: P42412

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)