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UniProtKB/Swiss-Prot entry Q7KW39


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MMSA_DROME
Primary accession number Q7KW39
Secondary accession numbers O46056 Q8T9I0 Q9V408
Integrated into Swiss-Prot on December 6, 2005
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 46)
Name and origin of the protein
Protein name Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial [Precursor]
Synonyms MMSDH
Malonate-semialdehyde dehydrogenase [acylating]
EC 1.2.1.27
EC 1.2.1.18
Gene name
ORFNames: CG17896
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
STRAIN=Oregon-R;
DOI=10.1126/science.287.5461.2220; PubMed=10731137 [NCBI, ExPASy, EBI, Israel, Japan]
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D. melanogaster.";
Science 287:2220-2222(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-520.
STRAIN=Berkeley;
TISSUE=Ovary;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE014298; AAF45510.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF45511.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL009147; CAA15632.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL009147; CAB41309.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069284; AAL39429.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T13418; T13418.
RefSeq NP_569845.2; -.
NP_726672.1; -.
UniGene Dm.11239
3D structure databases
HSSP P51977; 1BXS. [HSSP ENTRY / PDB]
ModBase Q7KW39.
Protein-protein interaction databases
IntAct Q7KW39; -.
Organism-specific databases
FlyBase FBgn0023537; CG17896.
Gene expression databases
ArrayExpress Q7KW39; -.
GermOnline CG17896; Drosophila melanogaster.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0000062; Molecular function: acyl-CoA binding (inferred from sequence or structural similarity from UniProtKB).
GO:0018478; Molecular function: malonate-semialdehyde dehydrogenase (acetylating) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004491; Molecular function: methylmalonate-semialdehyde dehydrogenase (acylating) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019859; Biological process: thymine metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006573; Biological process: valine metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR010061; MeMal-semiAld_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF27; MMSDH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01722; MMSDH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
ProtoNet Q7KW39.
Genome annotation databases
Ensembl CG17896; Drosophila melanogaster. [Contig view]
GeneID 30995; -.
KEGG dme:Dmel_CG17896; -.
Phylogenomic databases
HOGENOM Q7KW39; -.
Other
NextBio 771368; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   520        Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial. PRO_0000043373
NP_BIND   195   199  5     NAD (Potential). 
NP_BIND   247   252  6     NAD (Potential). 
ACT_SITE   303   303        Nucleophile (By similarity). 
BINDING   403   403        NAD (Potential). 
VAR_SEQ   2    10        Missing (in isoform A). VSP_051919
Sequence information
Length: 520 AA [This is the length of the unprocessed precursor] Molecular weight: 55972 Da [This is the MW of the unprocessed precursor] CRC64: 12AC03D9B9C3E41D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLVRLIGAE ARHLAKRSYS SAAPTTKLFI DGKFVESKTN EWIDVHDPAT NQVVTRVPKA 

        70         80         90        100        110        120 
TQAEMQAALE SNKKAFRSWS NQSILTRQQV MFKLQALIKE NMGELAKNIT KEQGKTLADA 

       130        140        150        160        170        180 
EGDVLRGLQV VEHCCSIPSL QMGETVANVA RDMDTYSLVL PLGVTAGVAP FNFPAMIPLW 

       190        200        210        220        230        240 
MFPVAITTGN TMLLKPSERV PGATMLLMEL LNEAGCPPGV VNVIHGQHDA VNFICDAPEI 

       250        260        270        280        290        300 
KAVSFVGSDQ AGKYIYERAG KNGKRVQSNM GAKNHGIILG DANKENTLNQ LAGAAFGAAG 

       310        320        330        340        350        360 
QRCMALSTAV FVGDAQAWIP DLVERAQKLK VNAGHVPGTD VGPVISAASR QRINDLIESG 

       370        380        390        400        410        420 
VKEGAKLILD GRKITVPGYE DGYFVGPTIL SDVTPSMKCY TEEIFGPVLV ILKADTLDDA 

       430        440        450        460        470        480 
IGIVNANPYG NGTAVFTTNG AAARKFVNEI DAGQVGVNVP IPVPLPMFSF TGTRGSFRGD 

       490        500        510        520 
HHFYGKQGIK FYTQTKTVTQ LWRKTDVTHT QAAVAMPTMK 

Q7KW39 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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