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P0C2X9 (AL4A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length563 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 By similarity.

Subcellular location

Mitochondrion matrix By similarity.

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 – 563540Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
PRO_0000287827

Regions

Nucleotide binding285 – 2895NAD By similarity

Sites

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

Amino acid modifications

Modified residue301N6-succinyllysine By similarity
Modified residue511N6-acetyllysine By similarity
Modified residue921N6-acetyllysine; alternate By similarity
Modified residue921N6-succinyllysine; alternate By similarity
Modified residue981N6-acetyllysine; alternate By similarity
Modified residue981N6-succinyllysine; alternate By similarity
Modified residue1131N6-acetyllysine; alternate By similarity
Modified residue1131N6-succinyllysine; alternate By similarity
Modified residue1291N6-acetyllysine; alternate By similarity
Modified residue1291N6-succinyllysine; alternate By similarity
Modified residue1741N6-acetyllysine; alternate By similarity
Modified residue1741N6-succinyllysine; alternate By similarity
Modified residue3171N6-acetyllysine By similarity
Modified residue3461N6-succinyllysine By similarity
Modified residue3641N6-acetyllysine By similarity
Modified residue3751N6-acetyllysine By similarity
Modified residue3941N6-succinyllysine By similarity
Modified residue4611N6-acetyllysine By similarity
Modified residue5081N6-acetyllysine; alternate By similarity
Modified residue5081N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C2X9 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: AF19417D93825EA5

FASTA56361,869
        10         20         30         40         50         60 
MLPPALLRRS LLSYAWRGSG LRWKHASSLK VANEPILAFT QGSPERDALQ KALNDLKDQT 

        70         80         90        100        110        120 
EAIPCVVGDE EVWTSDVRYQ LSPFNHGHKV AKFCYADKAL LNKAIEAAVL ARKEWDLKPV 

       130        140        150        160        170        180 
ADRAQIFLKA ADMLSGPRRA EILAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE 

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

       250        260        270        280        290        300 
SYAVYRILRE AGLPPNVIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWKQVAQN 

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

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

       430        440        450        460        470        480 
NESVGYFVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDE KYRETLQLVD STTSYGLTGA 

       490        500        510        520        530        540 
VFAQDKTIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGERDI PGQPRLVQLW 

       550        560 
TEPPFTPLAV SPPLGDWRYS YMQ 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 79-89 AND 318-337, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03107656 Genomic DNA. No translation available.
UniGeneRn.203318.

3D structure databases

ProteinModelPortalP0C2X9.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP0C2X9.
PRIDEP0C2X9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1624206. rat.

Organism-specific databases

RGD1624206. Aldh4a1.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271511.
HOVERGENHBG050484.
PhylomeDBP0C2X9.

Enzyme and pathway databases

SABIO-RKP0C2X9.
UniPathwayUPA00261; UER00374.

Gene expression databases

GenevestigatorP0C2X9.

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.
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...

Entry information

Entry nameAL4A1_RAT
AccessionPrimary (citable) accession number: P0C2X9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: April 16, 2014
This is version 57 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways