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Reviewed, UniProtKB/Swiss-Prot P28810 (MMSA_PSEAE)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Methylmalonate-semialdehyde dehydrogenase [acylating]
      Short name=MMSDH
    EC=1.2.1.27
Gene names
Name: mmsA
Ordered Locus Names: PA3570
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH.

Pathway

Amino-acid degradation; L-valine degradation.

Subunit structure

Homodimer.

Induction

By valine.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 497496Methylmalonate-semialdehyde dehydrogenase [acylating]
PRO_0000056584

Sites

Active site2821 By similarity

Sequences

Sequence LengthMass (Da)Tools
P28810-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3DB6BFC300AACA4D

FASTA49753,663
        10         20         30         40         50         60 
MSVPVRHLIA GAFVEGLGAQ RIPVSNPLDN STLAEIACAS AEQVEQAVAS ARETFASWKE 

        70         80         90        100        110        120 
TPVSERARVM LRYQALLKEH HDELAKIVSS ELGKTFEDAK GDVWRGIEVV EHACNVPSLL 

       130        140        150        160        170        180 
MGETVENVAR NIDTYSITQP LGVCVGITPF NFPAMIPLWM FPLAIACGNA FILKPSEQVP 

       190        200        210        220        230        240 
LTSVRLAELF LEAGAPKGVL QVVHGGKEQV DQLLKHPQVK AVSFVGSVAV GQYVYHTGTA 

       250        260        270        280        290        300 
HNKRVQSFAG AKNHMVIMPD ADKAQVISNL VGASVGAAGQ RCMAISVAVL VGAAREWIPE 

       310        320        330        340        350        360 
IRDALAKVRP GPWDDSGASY GPVINPQAKA RIERLIGQGV EEGAQLLLDG RGYKVEGYPD 

       370        380        390        400        410        420 
GNWVGPTLFA GVRPDMAIYR EEVFGPVLCL AEVDSLEQAI RLINESPYGN GTSIFTSSGA 

       430        440        450        460        470        480 
AARTFQHHIE VGQVGINIPI PVPLPFFSFT GWKGSFYGDL HAYGKQGVRF YTETKTVTAR 

       490 
WFDSDSVAGT NFSIQMR 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase."
Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R.
J. Biol. Chem. 267:13585-13592(1992) [PubMed: 1339433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"Biofouling in water treatment systems: effect of membrane properties on biofilm formation."
Liddor M.
Thesis (2005), Ben-Gurion University, Israel
Cited for: PROTEIN SEQUENCE OF 186-197 AND 335-351.
Strain: ATCC 33467 / type 1 smooth.

Cross-references

Sequence databases

M84911 Genomic DNA. Translation: AAA25891.1.
AE004091 Genomic DNA. Translation: AAG06958.1.
PIRB42902.
RefSeqNP_252260.1.

3D structure databases

HSSPHSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBaseSearch...

Genome annotation databases

GeneID878814.
GenomeReviewsGene locus PA3570 in contig AE004091_GR.
KEGGpae:PA3570.

Organism-specific databases

PseudoCAPPA3570.
CMRSearch...

Phylogenomic databases

HOGENOMP28810.
OMAP28810. ACASAEQ.

Enzyme and pathway databases

BioCycMetaCyc:MON-11663.
PAER208964:PA3570-MON.
BRENDA1.2.1.27. 354.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PTHR11699:SF27. MMSDH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01722. MMSDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMSA_PSEAE
AccessionPrimary (citable) accession number: P28810
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents