Reviewed, UniProtKB/Swiss-Prot Q29HB2 (MMSA_DROPS)

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

ORF Names:

GA14712

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Complete proteome]

Taxonomic identifier

46245 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	520 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 + H(2)O + NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA + CO(2) + NAD(P)H.
Subunit structure	Homotetramer By similarity.
Subcellular location	MitochondrionBy similarity.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
Sequence caution	The sequence EAL31846.1 differs from that shown. Reason: Erroneous gene model prediction.

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 thymine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB valine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acyl-CoA binding Inferred from sequence or structural similarity. Source: UniProtKB malonate-semialdehyde dehydrogenase (acetylating) activity Inferred from sequence or structural similarity. Source: UniProtKB methylmalonate-semialdehyde dehydrogenase (acylating) activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 520		Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial		PRO_0000312824
Regions
	Nucleotide binding	195 – 199	5	NAD Potential
	Nucleotide binding	247 – 252	6	NAD Potential
Sites
	Active site	303	1	Nucleophile By similarity
	Binding site	403	1	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	Q29HB2-1 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: E8336961D816B35D	FASTA	520	56,064
	10 20 30 40 50 60 MAFLRAIGAE ARYLTQRAYS SAAPTTKLFI DGKFVESKTK EWIDVHDPAT NKVVTRVPKA 70 80 90 100 110 120 TQDEMQTALE SNKKAFRSWS NQSILTRQAV MFKLQALIKE NMGELAKNIT KEQGKTLADA 130 140 150 160 170 180 EGDVLRGLQV VEHCCSIPSL QMGETVANVA RDMDTYSLVM PLGVTAGIAP FNFPAMIPLW 190 200 210 220 230 240 MFPVAITTGN TMLLKPSERV PGATMLLMEL LNEAGCPPGV VNVIHGQHDA VNFICDAPAI 250 260 270 280 290 300 KAVSFVGSDQ AGKYIYERAG KNGKRVQSNM GAKNHGVILS DANKENTLNQ LAGAAFGAAG 310 320 330 340 350 360 QRCMALSTAV FVGDAQGWIP DLVERAQKLK VNAGHVPGTD VGPVISAASR QRINDLIESG 370 380 390 400 410 420 VKEGAKLILD GRKISVPGFE DGYFVGPTIL SDVTPSMKCY TEEIFGPVLV ILKADNLDDA 430 440 450 460 470 480 IDIVNANPYG NGTAVFTTNG AAARKFVNEI DAGQVGVNVP IPVPLPMFSF TGTRGSFRGD 490 500 510 520 HHFYGKQGIK FYTQTKTVTQ LWRETDVNHT QAAVAMPTMK

References

[1]

"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution." Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L. , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A. Genome Res. 15:1-18(2005) [PubMed: 15632085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MV2-25.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH379064 Genomic DNA. Translation: EAL31846.1. Sequence problems.
RefSeq	XP_001354791.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4815188.
KEGG	dpo:Dpse_GA14712.
Organism-specific databases
FlyBase	FBgn0074739. Dpse\GA14712.
Family and domain databases
InterPro	IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. IPR010061. MeMal-semiAld_DHase. [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_DROPS

Accession

Primary (citable) accession number: Q29HB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	April 4, 2006
Last modified:	November 25, 2008
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project