Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q02253

- MMSA_RAT

UniProt

Q02253 - MMSA_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial

Gene

Aldh6a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.

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

  1. fatty-acyl-CoA binding Source: UniProtKB
  2. malonate-semialdehyde dehydrogenase (acetylating) activity Source: UniProtKB
  3. methylmalonate-semialdehyde dehydrogenase (acylating) activity Source: UniProtKB
  4. thiolester hydrolase activity Source: RGD

GO - Biological processi

  1. beta-alanine catabolic process Source: RGD
  2. thymine catabolic process Source: RGD
  3. thymine metabolic process Source: UniProtKB
  4. valine catabolic process Source: RGD
  5. valine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKQ02253.

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
Synonyms:Mmsdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621556. Aldh6a1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232Mitochondrion3 PublicationsAdd
BLAST
Chaini33 – 535503Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrialPRO_0000007190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471N6-acetyllysine; alternateBy similarity
Modified residuei47 – 471N6-succinyllysine; alternateBy similarity
Modified residuei52 – 521N6-acetyllysine; alternateBy similarity
Modified residuei52 – 521N6-succinyllysine; alternateBy similarity
Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
Modified residuei87 – 871N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-acetyllysine; alternateBy similarity
Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei298 – 2981N6-acetyllysineBy similarity
Modified residuei330 – 3301N6-acetyllysineBy similarity
Modified residuei331 – 3311N6-acetyllysineBy similarity
Modified residuei364 – 3641N6-acetyllysine; alternateBy similarity
Modified residuei364 – 3641N6-succinyllysine; alternateBy similarity
Modified residuei376 – 3761N6-acetyllysine; alternateBy similarity
Modified residuei376 – 3761N6-succinyllysine; alternateBy similarity
Modified residuei391 – 3911N6-succinyllysineBy similarity
Modified residuei500 – 5001N6-acetyllysineBy similarity
Modified residuei517 – 5171N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ02253.
PRIDEiQ02253.

Expressioni

Tissue specificityi

Expressed in the head and flagellum of epididymal sperm but not in testicular sperm (at protein level). Kidney > liver > heart > muscle > brain.1 Publication

Gene expression databases

GenevestigatoriQ02253.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiQ02253. 1 interaction.
STRINGi10116.ENSRNOP00000015545.

Structurei

3D structure databases

ProteinModelPortaliQ02253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271507.
HOVERGENiHBG105023.
InParanoidiQ02253.
KOiK00140.
PhylomeDBiQ02253.

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:SF27. PTHR11699:SF27. 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.

Q02253-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAVAAAAA VRSRILQVSS KVNSTWYPAS SFSSSSVPTV KLFIDGKFVE
60 70 80 90 100
SKSDKWIDIH NPATNEVVGR VPQSTKAEME AAVAACKRAF 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 QHEAVNFICD
260 270 280 290 300
HPDIKAISFV GSNQAGEYIF ERGSRNGKRV QANMGAKNHG VVMPDANKEN
310 320 330 340 350
TLNQLVGAAF GAAGQRCMAL STAVLVGEAK KWLPELVERA KNLRVNAGDQ
360 370 380 390 400
PGADLGPLIT PQAKERVCNL IDSGAKEGAS ILLDGRKIKV KGYENGNFVG
410 420 430 440 450
PTIISNVKPS MTCYKEEIFG PVLVVLETET LDEAIKIVND NPYGNGTAIF
460 470 480 490 500
TTNGAIARKY AHMVDVGQVG VNVPIPVPLP MFSFTGSRSS FRGDTNFYGK
510 520 530
QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR
Length:535
Mass (Da):57,808
Last modified:July 1, 1993 - v1
Checksum:iD914CE0311AA466A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451D → N AA sequence (PubMed:1527093)Curated
Sequence conflicti50 – 501E → Q AA sequence (PubMed:1527093)Curated
Sequence conflicti166 – 1661D → N AA sequence (PubMed:1527093)Curated
Sequence conflicti168 – 1681D → N AA sequence (PubMed:1527093)Curated
Sequence conflicti184 – 1841P → T AA sequence (PubMed:1527093)Curated
Sequence conflicti190 – 1901M → G AA sequence (PubMed:1527093)Curated

Mass spectrometryi

Molecular mass is 57770.57 Da from positions 1 - 535. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93401 mRNA. Translation: AAA41638.1.
PIRiA44097.
RefSeqiNP_112319.2. NM_031057.2.
UniGeneiRn.2098.

Genome annotation databases

GeneIDi81708.
KEGGirno:81708.
UCSCiRGD:621556. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93401 mRNA. Translation: AAA41638.1 .
PIRi A44097.
RefSeqi NP_112319.2. NM_031057.2.
UniGenei Rn.2098.

3D structure databases

ProteinModelPortali Q02253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q02253. 1 interaction.
STRINGi 10116.ENSRNOP00000015545.

Proteomic databases

PaxDbi Q02253.
PRIDEi Q02253.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81708.
KEGGi rno:81708.
UCSCi RGD:621556. rat.

Organism-specific databases

CTDi 4329.
RGDi 621556. Aldh6a1.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271507.
HOVERGENi HBG105023.
InParanoidi Q02253.
KOi K00140.
PhylomeDBi Q02253.

Enzyme and pathway databases

SABIO-RK Q02253.

Miscellaneous databases

NextBioi 615332.
PROi Q02253.

Gene expression databases

Genevestigatori Q02253.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. 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 ]
PANTHERi PTHR11699:SF27. PTHR11699:SF27. 1 hit.
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01722. MMSDH. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution."
    Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A.
    J. Biol. Chem. 267:19724-19729(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-50 AND 166-190.
    Tissue: Liver.
  2. "Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase."
    Goodwin G.W., Rougraff P.M., Davis E.J., Harris R.A.
    J. Biol. Chem. 264:14965-14971(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-50, CHARACTERIZATION.
  3. "The effect of ligand binding on the proteolytic pattern of methylmalonate semialdehyde dehydrogenase."
    Kedishvili N.Y., Popov K.M., Harris R.A.
    Arch. Biochem. Biophys. 290:21-26(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 56-70, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  5. "Differential proteomics leads to identification of domain specific epididymal sperm proteins."
    Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.
    J. Androl. 32:240-259(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, MASS SPECTROMETRY.
    Strain: Holtzman.
    Tissue: Sperm.

Entry informationi

Entry nameiMMSA_RAT
AccessioniPrimary (citable) accession number: Q02253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 124 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3