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Protein

Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial

Gene

Aldh6a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity).By similarity

Catalytic activityi

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH.
3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei317 – 3171NucleophilePROSITE-ProRule annotation
Binding sitei417 – 4171NADSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi209 – 2135NADSequence analysis
Nucleotide bindingi261 – 2666NADSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.18. 3474.
ReactomeiR-MMU-70895. Branched-chain amino acid catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (EC:1.2.1.18, EC:1.2.1.27)
Short name:
MMSDH
Short name:
Malonate-semialdehyde dehydrogenase [acylating]
Alternative name(s):
Aldehyde dehydrogenase family 6 member A1
Gene namesi
Name:Aldh6a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1915077. Aldh6a1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionBy similarityAdd
BLAST
Chaini33 – 535503Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrialPRO_0000320299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471N6-acetyllysine; alternateCombined sources
Modified residuei47 – 471N6-succinyllysine; alternateCombined sources
Modified residuei52 – 521N6-acetyllysine; alternateCombined sources
Modified residuei52 – 521N6-succinyllysine; alternateCombined sources
Modified residuei55 – 551N6-acetyllysine; alternateCombined sources
Modified residuei55 – 551N6-succinyllysine; alternateCombined sources
Modified residuei76 – 761N6-acetyllysine; alternateCombined sources
Modified residuei76 – 761N6-succinyllysine; alternateCombined sources
Modified residuei87 – 871N6-acetyllysineCombined sources
Modified residuei117 – 1171N6-acetyllysine; alternateCombined sources
Modified residuei117 – 1171N6-succinyllysine; alternateCombined sources
Modified residuei129 – 1291N6-acetyllysine; alternateCombined sources
Modified residuei129 – 1291N6-succinyllysine; alternateCombined sources
Modified residuei262 – 2621PhosphoserineBy similarity
Modified residuei298 – 2981N6-acetyllysineCombined sources
Modified residuei330 – 3301N6-acetyllysineCombined sources
Modified residuei331 – 3311N6-acetyllysineCombined sources
Modified residuei364 – 3641N6-acetyllysine; alternateCombined sources
Modified residuei364 – 3641N6-succinyllysine; alternateCombined sources
Modified residuei376 – 3761N6-acetyllysine; alternateCombined sources
Modified residuei376 – 3761N6-succinyllysine; alternateCombined sources
Modified residuei380 – 3801PhosphoserineBy similarity
Modified residuei391 – 3911N6-succinyllysineCombined sources
Modified residuei500 – 5001N6-acetyllysineCombined sources
Modified residuei517 – 5171N6-succinyllysineCombined sources

Post-translational modificationi

Acetylation of Lys-55; Lys-117 and Lys-331 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9EQ20.
MaxQBiQ9EQ20.
PaxDbiQ9EQ20.
PeptideAtlasiQ9EQ20.
PRIDEiQ9EQ20.

2D gel databases

REPRODUCTION-2DPAGEQ8CIB4.
Q9EQ20.

PTM databases

iPTMnetiQ9EQ20.
PhosphoSiteiQ9EQ20.
SwissPalmiQ9EQ20.

Expressioni

Gene expression databases

BgeeiQ9EQ20.
CleanExiMM_ALDH6A1.
GenevisibleiQ9EQ20. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi222701. 1 interaction.
IntActiQ9EQ20. 4 interactions.
MINTiMINT-1860357.
STRINGi10090.ENSMUSP00000082288.

Structurei

3D structure databases

ProteinModelPortaliQ9EQ20.
SMRiQ9EQ20. Positions 9-516.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2449. Eukaryota.
ENOG410XNP1. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271507.
HOVERGENiHBG105023.
InParanoidiQ9EQ20.
KOiK00140.
OMAiSNVKPNM.
OrthoDBiEOG7J70F8.
PhylomeDBiQ9EQ20.
TreeFamiTF105651.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
PANTHERiPTHR11699:SF183. PTHR11699:SF183. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01722. MMSDH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EQ20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVAAAAA MRSRILQVSS KVNATWYPAS SFSSSSVPTV KLFIDGKFVE
60 70 80 90 100
SKSDKWIDIH NPATNEVVGR VPQSTKAEMD AAVESCKRAF PAWADTSILS
110 120 130 140 150
RQQVLLRYQQ LIKENLKEIA RLITLEQGKT LADAEGDVFR GLQVVEHACS
160 170 180 190 200
VTSLMLGETM PSITKDMDLY SYRLPLGVCA GIAPFNFPAM IPLWMFPMAM
210 220 230 240 250
VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG QHDAVNFICD
260 270 280 290 300
HPDIKAISFV GSNQAGEYIF ERGSRNGKRV QANMGAKNHG VVMPDANKEN
310 320 330 340 350
TLNQLVGAAF GAAGQRCMAL STAILVGEAK KWLPELVDRA KNLRVNAGDQ
360 370 380 390 400
PGADLGPLIT PQAKERVCNL IDSGTKEGAS ILLDGRRIKV KGYENGNFVG
410 420 430 440 450
PTIISNVKPS MTCYKEEIFG PVLVVLETET LDEAIKIVND NPYGNGTAIF
460 470 480 490 500
TTNGATARKY AHMVDVGQVG VNVPIPVPLP MFSFTGSRSS FRGDTNFYGK
510 520 530
QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR
Length:535
Mass (Da):57,916
Last modified:March 1, 2001 - v1
Checksum:i1EF4ED4C4FE2284D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551K → R in BAE41702 (PubMed:16141072).Curated
Sequence conflicti141 – 1411G → C in AAH33440 (PubMed:15489334).Curated
Sequence conflicti211 – 2111S → P in BAE41702 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297860 mRNA. Translation: AAG44988.1.
AK033587 mRNA. Translation: BAC28375.1.
AK147146 mRNA. Translation: BAE27715.1.
AK155814 mRNA. Translation: BAE33445.1.
AK169915 mRNA. Translation: BAE41455.1.
AK170305 mRNA. Translation: BAE41702.1.
AK171581 mRNA. Translation: BAE42539.1.
AK171896 mRNA. Translation: BAE42726.1.
BC033440 mRNA. Translation: AAH33440.1.
CCDSiCCDS26046.1.
RefSeqiNP_598803.1. NM_134042.3.
UniGeneiMm.247510.

Genome annotation databases

EnsembliENSMUST00000085192; ENSMUSP00000082288; ENSMUSG00000021238.
GeneIDi104776.
KEGGimmu:104776.
UCSCiuc007ofk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297860 mRNA. Translation: AAG44988.1.
AK033587 mRNA. Translation: BAC28375.1.
AK147146 mRNA. Translation: BAE27715.1.
AK155814 mRNA. Translation: BAE33445.1.
AK169915 mRNA. Translation: BAE41455.1.
AK170305 mRNA. Translation: BAE41702.1.
AK171581 mRNA. Translation: BAE42539.1.
AK171896 mRNA. Translation: BAE42726.1.
BC033440 mRNA. Translation: AAH33440.1.
CCDSiCCDS26046.1.
RefSeqiNP_598803.1. NM_134042.3.
UniGeneiMm.247510.

3D structure databases

ProteinModelPortaliQ9EQ20.
SMRiQ9EQ20. Positions 9-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222701. 1 interaction.
IntActiQ9EQ20. 4 interactions.
MINTiMINT-1860357.
STRINGi10090.ENSMUSP00000082288.

PTM databases

iPTMnetiQ9EQ20.
PhosphoSiteiQ9EQ20.
SwissPalmiQ9EQ20.

2D gel databases

REPRODUCTION-2DPAGEQ8CIB4.
Q9EQ20.

Proteomic databases

EPDiQ9EQ20.
MaxQBiQ9EQ20.
PaxDbiQ9EQ20.
PeptideAtlasiQ9EQ20.
PRIDEiQ9EQ20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085192; ENSMUSP00000082288; ENSMUSG00000021238.
GeneIDi104776.
KEGGimmu:104776.
UCSCiuc007ofk.2. mouse.

Organism-specific databases

CTDi4329.
MGIiMGI:1915077. Aldh6a1.

Phylogenomic databases

eggNOGiKOG2449. Eukaryota.
ENOG410XNP1. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271507.
HOVERGENiHBG105023.
InParanoidiQ9EQ20.
KOiK00140.
OMAiSNVKPNM.
OrthoDBiEOG7J70F8.
PhylomeDBiQ9EQ20.
TreeFamiTF105651.

Enzyme and pathway databases

BRENDAi1.2.1.18. 3474.
ReactomeiR-MMU-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

PROiQ9EQ20.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQ20.
CleanExiMM_ALDH6A1.
GenevisibleiQ9EQ20. MM.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
PANTHERiPTHR11699:SF183. PTHR11699:SF183. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01722. MMSDH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse methylmalonate-semialdehyde dehydrogenase (MMSDH) cDNA and gene map."
    Yang B.-Z., Zhang L.-F., Roe C.R., Ding J.-H.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cecum, Kidney and Spleen.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-52; LYS-55; LYS-76; LYS-117; LYS-129; LYS-364; LYS-376; LYS-391 AND LYS-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-52; LYS-55; LYS-76; LYS-87; LYS-117; LYS-129; LYS-298; LYS-330; LYS-331; LYS-364; LYS-376 AND LYS-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMMSA_MOUSE
AccessioniPrimary (citable) accession number: Q9EQ20
Secondary accession number(s): Q3TDA2, Q8CIB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.