Reviewed, UniProtKB/Swiss-Prot Q54I10 (MMSA_DICDI)

Names and origin

Protein names

Recommended name:
    Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
      Short name=MMSDH
      Short name=Malonate-semialdehyde dehydrogenase [acylating]
    EC=1.2.1.27
    EC=1.2.1.18

Gene names

Name:	mmsdh
Synonyms:	aldh6
ORF Names:	DDB_G0289085

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA By similarity.
Catalytic activity	2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH. 3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW valine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	malonate-semialdehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: EC methylmalonate-semialdehyde dehydrogenase (acylating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Potential
	Chain	27 – 528	502	Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial		PRO_0000327926
Regions
	Nucleotide binding	199 – 203	5	NAD Potential
	Nucleotide binding	251 – 256	6	NAD Potential
Sites
	Active site	307	1	Nucleophile By similarity
	Binding site	408	1	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54I10-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: D83629D894CC3E68	FASTA	528	56,696
	10 20 30 40 50 60 MLSFKFAKSA SKVIGNRNFH SSSASLANTT KLFINGKFVE SKTKEWLEVR NPATQELVTK 70 80 90 100 110 120 VPVSTKEEME AAVKAASDAF PAWRDTSVSN RSRIISNYKN LINKNMDKIA AIITEEQGKT 130 140 150 160 170 180 LPDAKGDVFR GLEVVEHSVN VASLMMGETV ENVSKNVDIY SYVQPLGVCA GITPFNFPAM 190 200 210 220 230 240 IPLWMFPLAI ACGNTFVLKP SERVPSASMF LVQLAQEAGV PDGVVNVIHG GKEAVNFICD 250 260 270 280 290 300 APEVRAISFV GADQAGRHIH ARGTANGKRV QSNMAAKNHA TIVPDAHKER TLDALTGAAF 310 320 330 340 350 360 GASGQRCMAL SAAVFVGESK NWIPELAERA KKLKVAGGAA PGADLGPVIS AASKQRIHEL 370 380 390 400 410 420 IQSGIDEGAK CILDGRNVVV DPEFSKGNFV GPTILTDVKP HMRCYKEEIF GPVLVCLNVD 430 440 450 460 470 480 TVDQAIQLIN ANPYGNGTAV FTSSGAVARK YQREIDVGQV GINLPIPVPL PFFSFTGSRG 490 500 510 520 SFVGAGHFYG KTGVQFFTQI KTITSNWRDD DISHGVSSSM NMPILGKN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000130 Genomic DNA. Translation: EAL62892.1.
RefSeq	XP_636395.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3387978.
KEGG	ddi:DDB_0231483.
Organism-specific databases
dictyBase	DDB_G0289085. mmsdh.
Phylogenomic databases
OMA	Q54I10. IISNVKP.
Enzyme and pathway databases
BRENDA	1.2.1.18. 424. 1.2.1.27. 424.
Family and domain databases
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

MMSA_DICDI

Accession

Primary (citable) accession number: Q54I10

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)