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Reviewed, UniProtKB/Swiss-Prot Q9DBF1 (AL7A1_MOUSE)

Last modified January 19, 2010. Version 75. 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:
    Alpha-aminoadipic semialdehyde dehydrogenase
      Short name=Alpha-AASA dehydrogenase
    EC=1.2.1.31
Alternative name(s):
    Delta1-piperideine-6-carboxylate dehydrogenease
      Short name=P6c dehydrogenase
    Aldehyde dehydrogenase family 7 member A1
    Antiquitin-1
Gene names
Name: Aldh7a1
Synonyms: Ald7a1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.

Subunit structure

Homotetramer By similarity. UniProtKB P83402

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionL-aminoadipate-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity UniProtKB P83402
Chain2 – 511510Alpha-aminoadipic semialdehyde dehydrogenase
PRO_0000056491

Regions

Nucleotide binding246 – 2516NAD By similarity UniProtKB Q56694

Sites

Active site2681Proton acceptor By similarity UniProtKB Q56694
Active site3021Nucleophile By similarity UniProtKB Q56694
Site1671Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DBF1-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 37952CEC7C5F3A85

FASTA51155,645
        10         20         30         40         50         60 
MSTLLIHHPQ YAWLQDLGLR EDNEGVYNGS WGGRGEVITT YCPANNEPIA RVRQASLKDY 

        70         80         90        100        110        120 
EETIGKAKKA WNIWADIPAP KRGEIVRKIG DAFREKIQLL GRLVSLEMGK ILVEGIGEVQ 

       130        140        150        160        170        180 
EYVDVCDYAA GLSRMIGGPT LPSERPGHAL IEMWNPLGLV GIITAFNFPV AVFGWNNAIA 

       190        200        210        220        230        240 
LITGNVCLWK GAPTTSLVSV AVTKIIAQVL EDNLLPGAIC SLVCGGADIG TTMARDERVN 

       250        260        270        280        290        300 
LLSFTGSTQV GKEVALMVQE RFGKSLLELG GNNAIIAFED ADLSLVVPSV LFAAVGTAGQ 

       310        320        330        340        350        360 
RCTTVRRLFL HESIHNEVVD RLRSAYSQIR VGNPWDPNIL YGPLHTKQAV SMFVRAVEEA 

       370        380        390        400        410        420 
KKQGGTVVYG GKVMDHPGNY VEPTIVTGLA HDAPIVHQET FAPILYVFKF QDEEEVFEWN 

       430        440        450        460        470        480 
NEVKQGLSSS IFTKDLGRIF RWLGPKGSDC GIVNVNIPTS GAEIGGAFGG EKHTGGGRES 

       490        500        510 
GSDAWKQYMR RSTCTINYST SLPLAQGIKF Q 

« Hide

References

[1]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004991 mRNA. Translation: BAB23726.1.
BC012407 mRNA. Translation: AAH12407.1.
IPIIPI00890092.
RefSeqNP_001120810.1.
NP_613066.2.
UniGeneMm.30250

3D structure databases

SMRQ9DBF1. Positions 2-499.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DBF1.

2-D gel databases

REPRODUCTION-2DPAGEQ9DBF1.

Proteomic databases

PRIDEQ9DBF1.

Genome annotation databases

EnsemblENSMUST00000066208; ENSMUSP00000065089; ENSMUSG00000053644; Mus musculus. [Genome view]
ENSMUST00000116635; ENSMUSP00000112334; ENSMUSG00000053644; Mus musculus. [Genome view]
GeneID110695.
KEGGmmu:110695.
NMPDRfig|10090.3.peg.4006.
UCSCuc008eyo.1. mouse.

Organism-specific databases

CTD110695.
MGIMGI:108186. Aldh7a1.

Phylogenomic databases

HOVERGENQ9DBF1.
InParanoidQ9DBF1.
OMAWNPLGVV.
OrthoDBEOG99KJ9G.
PhylomeDBQ9DBF1.

Enzyme and pathway databases

BRENDA1.2.1.31. 244.

Gene expression databases

ArrayExpressQ9DBF1.
BgeeQ9DBF1.
CleanExMM_ALDH7A1.
GenevestigatorQ9DBF1.
GermOnlineENSMUSG00000053644. Mus musculus.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio364487.
SOURCESearch...

Entry information

Entry nameAL7A1_MOUSE
AccessionPrimary (citable) accession number: Q9DBF1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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