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Q8CHT0 (AL4A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Short name=P5C dehydrogenase
EC=1.2.1.88
Alternative name(s):
Aldehyde dehydrogenase family 4 member A1
L-glutamate gamma-semialdehyde dehydrogenase
Gene names
Name:Aldh4a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes By similarity.

Catalytic activity

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.

Subunit structure

Homodimer. Ref.8

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion By similarity
Chain24 – 562539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
PRO_0000007174

Regions

Nucleotide binding285 – 2895NAD

Sites

Active site3131Proton acceptor Ref.8
Active site3471Nucleophile Ref.8
Binding site2071NAD
Binding site2321NAD
Binding site4461NAD
Binding site5121Substrate
Site2101Transition state stabilizer By similarity

Amino acid modifications

Modified residue301N6-succinyllysine Ref.5
Modified residue511N6-acetyllysine Ref.6
Modified residue921N6-acetyllysine; alternate Ref.6
Modified residue921N6-succinyllysine; alternate Ref.5
Modified residue981N6-acetyllysine; alternate Ref.6
Modified residue981N6-succinyllysine; alternate Ref.5
Modified residue1131N6-acetyllysine; alternate Ref.6
Modified residue1131N6-succinyllysine; alternate Ref.5
Modified residue1291N6-acetyllysine; alternate Ref.6
Modified residue1291N6-succinyllysine; alternate Ref.5
Modified residue1741N6-acetyllysine; alternate Ref.6
Modified residue1741N6-succinyllysine; alternate Ref.5
Modified residue3171N6-acetyllysine Ref.6
Modified residue3461N6-succinyllysine Ref.5
Modified residue3571N6-acetyllysine; alternate Ref.6
Modified residue3571N6-succinyllysine; alternate Ref.5
Modified residue3641N6-acetyllysine Ref.6
Modified residue3751N6-acetyllysine Ref.6
Modified residue3941N6-succinyllysine Ref.5
Modified residue4611N6-acetyllysine Ref.6
Modified residue5081N6-acetyllysine; alternate Ref.6
Modified residue5081N6-succinyllysine; alternate Ref.5
Modified residue5301N6-acetyllysine Ref.6
Modified residue5511N6-acetyllysine Ref.6

Experimental info

Sequence conflict181G → S in BAC32045. Ref.1
Sequence conflict181G → S in AAH56226. Ref.4
Sequence conflict181G → S in AAH39281. Ref.4
Sequence conflict181G → S in AAH24133. Ref.4
Sequence conflict321T → A in BAC32045. Ref.1
Sequence conflict321T → A in AAH56226. Ref.4
Sequence conflict321T → A in AAH39281. Ref.4
Sequence conflict321T → A in AAH24133. Ref.4
Sequence conflict471D → G in BAC32045. Ref.1
Sequence conflict601M → T in BAC32045. Ref.1
Sequence conflict601M → T in AAH56226. Ref.4
Sequence conflict601M → T in AAH39281. Ref.4
Sequence conflict601M → T in AAH24133. Ref.4
Sequence conflict4671Q → K in BAC32045. Ref.1
Sequence conflict4671Q → K in AAH56226. Ref.4
Sequence conflict4671Q → K in AAH39281. Ref.4
Sequence conflict4671Q → K in AAH24133. Ref.4
Sequence conflict4671Q → K in AAH26589. Ref.4

Secondary structure

.................................................................................... 562
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CHT0 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 4D8A0C9C68A99478

FASTA56261,841
        10         20         30         40         50         60 
MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ KALKDLKGQM 

        70         80         90        100        110        120 
EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL LNRAIDAALA ARKEWDLKPM 

       130        140        150        160        170        180 
ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE 

       190        200        210        220        230        240 
GEQPISVPPS TNHTVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA 

       250        260        270        280        290        300 
SYAVYRILRE AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN 

       310        320        330        340        350        360 
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPKSLW 

       370        380        390        400        410        420 
PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC 

       430        440        450        460        470        480 
NESVGYYVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDD KYRETLQLVD STTSYGLTGA 

       490        500        510        520        530        540 
VFAQDKAIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW 

       550        560 
TSPQVIKETH KPLGDWRYSY MQ 

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Retina.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Kidney and Liver.
[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-30; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-346; LYS-357; LYS-394 AND LYS-508, 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-51; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-317; LYS-357; LYS-364; LYS-375; LYS-461; LYS-508; LYS-530 AND LYS-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Proline: Mother Nature's cryoprotectant applied to protein crystallography."
Pemberton T.A., Still B.R., Christensen E.M., Singh H., Srivastava D., Tanner J.J.
Acta Crystallogr. D 68:1010-1018(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 21-562.
[8]"The three-dimensional structural basis of type II hyperprolinemia."
Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., Tanner J.J.
J. Mol. Biol. 420:176-189(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-562 IN COMPLEXES WITH GLUTAMATE AND NAD, SUBUNIT, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK044712 mRNA. Translation: BAC32045.1.
AL831790 Genomic DNA. Translation: CAM21310.1.
CH466615 Genomic DNA. Translation: EDL13315.1.
BC024133 mRNA. Translation: AAH24133.1.
BC026589 mRNA. Translation: AAH26589.1.
BC039281 mRNA. Translation: AAH39281.2.
BC056226 mRNA. Translation: AAH56226.1.
CCDSCCDS18848.1.
RefSeqNP_780647.3. NM_175438.4.
UniGeneMm.273571.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V9JX-ray1.30A/B21-562[»]
3V9KX-ray1.50A/B21-562[»]
3V9LX-ray1.50A/B21-562[»]
4E3XX-ray1.24A/B21-562[»]
4LGZX-ray1.68A/B21-562[»]
4LH0X-ray1.67A/B21-562[»]
4LH1X-ray1.67A/B21-562[»]
4LH2X-ray1.67A/B21-562[»]
4LH3X-ray1.81A/B21-562[»]
ProteinModelPortalQ8CHT0.
SMRQ8CHT0. Positions 21-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CHT0. 3 interactions.
MINTMINT-1859863.

PTM databases

PhosphoSiteQ8CHT0.

Proteomic databases

MaxQBQ8CHT0.
PaxDbQ8CHT0.
PRIDEQ8CHT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737.
GeneID212647.
KEGGmmu:212647.
UCSCuc012dnu.1. mouse.

Organism-specific databases

CTD8659.
MGIMGI:2443883. Aldh4a1.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00560000077335.
HOGENOMHOG000271511.
HOVERGENHBG050484.
InParanoidB1AXW8.
KOK00294.
OMALRWKHTS.
OrthoDBEOG7T1R9D.
TreeFamTF300481.

Enzyme and pathway databases

UniPathwayUPA00261; UER00374.

Gene expression databases

ArrayExpressQ8CHT0.
BgeeQ8CHT0.
CleanExMM_ALDH4A1.
GenevestigatorQ8CHT0.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR005931. 1-pyrroline-5-COlate_DH.
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH4A1. mouse.
NextBio373656.
PROQ8CHT0.
SOURCESearch...

Entry information

Entry nameAL4A1_MOUSE
AccessionPrimary (citable) accession number: Q8CHT0
Secondary accession number(s): B1AXW8 expand/collapse secondary AC list , Q7TND0, Q8BXM3, Q8R0N1, Q8R1S2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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