Reviewed, UniProtKB/Swiss-Prot Q8Y9Y4 (IOLA_LISMO)

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
Ordered Locus Names:	lmo0383

Organism

Listeria monocytogenes [Complete proteome] [HAMAP]

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Converts malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively By similarity. HAMAP MF_01670
Catalytic activity	3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H. HAMAP MF_01670 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH. HAMAP MF_01670
Pathway	Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7. HAMAP MF_01670
Subunit structure	Homotetramer By similarity. HAMAP MF_01670
Sequence similarities	Belongs to the aldehyde dehydrogenase family. IolA subfamily.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	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 – 488	488	Methylmalonate semialdehyde dehydrogenase [acylating] HAMAP MF_01670		PRO_0000352346
Regions
	Nucleotide binding	176 – 180	5	NAD By similarity
Sites
	Active site	284	1	Nucleophile By similarity
	Binding site	382	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y9Y4-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 2E663708E37A0698	FASTA	488	53,321
	10 20 30 40 50 60 MADVRKLKNY IDGEWVESKT DKYEDVINPA TGEVLCQVPI STRAELDQAA VIAEQAFEKW 70 80 90 100 110 120 SQVAVPRRAR VLFGFQQLLI QHKEELARLI TLENGKNLSE ARGEVQRGIE NVEFAAGAPT 130 140 150 160 170 180 LMMGDSLASI ATDVEAANYR YPVGVVGGIA PFNFPMMVPC WMFPMAIALG NSFILKPSER 190 200 210 220 230 240 TPLLMEKLVE LFSEAGLPKG VFNVVYGAHD VVNGILENEI IKAVSFVGSK PVGEYVYKTG 250 260 270 280 290 300 SANLKRVQAL TGAKNHTIVL NDADLEDTVT NVISAAFGSA GERCMACAVV TVEEGIADEF 310 320 330 340 350 360 LEALRTAAQN VKIGNGLDDG VFLGPVIREE NQKRTIAYIE KGIEEGAKLT VDGRETGLSE 370 380 390 400 410 420 GHFVGPTILE DVTTDMTIWK DEIFAPVLSV IRVKNLQEAV RVANQSEFAN GACIFTNNAK 430 440 450 460 470 480 AIRYFREKID AGMLGVNLGV PAPMAFFPFS GWKSSFYGTL HANGKDSVDF YTHKKVVTAR YSLKGYEE

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591975 Genomic DNA. Translation: CAC98462.1.
PIR	AH1122.
RefSeq	NP_463913.1.
3D structure databases
HSSP	HSSP built from PDB template 1T90 based on UniProtKB P42412.
SMR	Q8Y9Y4. Positions 3-481.
ModBase	Search...
Genome annotation databases
GeneID	987639.
KEGG	lmo:lmo0383.
Organism-specific databases
ListiList	LMO0383.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG752218.
OMA	HIYTTAS.
Enzyme and pathway databases
BioCyc	LMON169963:LMO0383-MONOMER.
Family and domain databases
HAMAP	MF_01670. IolA. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. 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_LISMO

Accession

Primary (citable) accession number: Q8Y9Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 44 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)