Reviewed, UniProtKB/Swiss-Prot Q92EQ7 (IOLA_LISIN)

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:	lin0401

Organism

Listeria innocua [Complete proteome] [HAMAP]

Taxonomic identifier

1642 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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_0000352345
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)
	Q92EQ7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 787B0C3D6EC7026C	FASTA	488	53,248
	10 20 30 40 50 60 MADVRKLKNY INGEWVESKA DKYEDVINPA TGEVLCQVPI STRAELDQAA VIAEQAFEKW 70 80 90 100 110 120 SQVAVPRRAR VLFSFQQLLI 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 VVNGILENET IKAVSFVGSK PVGEYVYKTG 250 260 270 280 290 300 SANLKRVQAL TGAKNHTIVL NDADLEDTVT NVISAAFGSA GERCMACAVV TVEEGIADDF 310 320 330 340 350 360 LAALRTAAQN VKIGNGLDDG VFLGPVIREE NQKRTIAYIE KGVEEGAKLT VDGRETGLSE 370 380 390 400 410 420 GYFVGPTILE 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: CLIP 11262 / Serovar 6a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL596164 Genomic DNA. Translation: CAC95634.1.
PIR	AB1483.
RefSeq	NP_469746.1.
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
SMR	Q92EQ7. Positions 3-481.
ModBase	Search...
Genome annotation databases
GeneID	1128839.
GenomeReviews	Gene locus lin0401 in contig AL592022_GR.
KEGG	lin:lin0401.
NMPDR	fig|272626.1.peg.399.
Organism-specific databases
ListiList	LIN0401.
CMR	Search...
Phylogenomic databases
HOGENOM	Q92EQ7.
OMA	Q92EQ7. ASNDFGP.
Enzyme and pathway databases
BioCyc	LINN272626:LIN0401-MONOMER.
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_LISIN

Accession

Primary (citable) accession number: Q92EQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 41 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)