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P0C2X9

- AL4A1_RAT

UniProt

P0C2X9 - AL4A1_RAT

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Protein

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Gene

Aldh4a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei207 – 2071NADBy similarity
Sitei210 – 2101Transition state stabilizerBy similarity
Binding sitei232 – 2321NADBy similarity
Active sitei313 – 3131Proton acceptorPROSITE-ProRule annotation
Active sitei347 – 3471NucleophilePROSITE-ProRule annotation
Binding sitei446 – 4461NADBy similarity
Binding sitei512 – 5121SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 2895NADBy similarity

GO - Molecular functioni

  1. 1-pyrroline-5-carboxylate dehydrogenase activity Source: InterPro
  2. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. glutamate biosynthetic process Source: InterPro
  2. proline biosynthetic process Source: InterPro
  3. proline catabolic process to glutamate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP0C2X9.
UniPathwayiUPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
Short name:
P5C dehydrogenase
Alternative name(s):
Aldehyde dehydrogenase family 4 member A1
L-glutamate gamma-semialdehyde dehydrogenase
Gene namesi
Name:Aldh4a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1624206. Aldh4a1.

Subcellular locationi

Mitochondrion matrix By similarity

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 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 563540Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialPRO_0000287827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-succinyllysineBy similarity
Modified residuei51 – 511N6-acetyllysineBy similarity
Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
Modified residuei98 – 981N6-acetyllysine; alternateBy similarity
Modified residuei98 – 981N6-succinyllysine; alternateBy similarity
Modified residuei113 – 1131N6-acetyllysine; alternateBy similarity
Modified residuei113 – 1131N6-succinyllysine; alternateBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei174 – 1741N6-acetyllysine; alternateBy similarity
Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity
Modified residuei317 – 3171N6-acetyllysineBy similarity
Modified residuei346 – 3461N6-succinyllysineBy similarity
Modified residuei364 – 3641N6-acetyllysineBy similarity
Modified residuei375 – 3751N6-acetyllysineBy similarity
Modified residuei394 – 3941N6-succinyllysineBy similarity
Modified residuei461 – 4611N6-acetyllysineBy similarity
Modified residuei508 – 5081N6-acetyllysine; alternateBy similarity
Modified residuei508 – 5081N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0C2X9.
PRIDEiP0C2X9.

Expressioni

Gene expression databases

GenevestigatoriP0C2X9.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP0C2X9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271511.
HOVERGENiHBG050484.
InParanoidiP0C2X9.
PhylomeDBiP0C2X9.

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.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C2X9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPPALLRRS LLSYAWRGSG LRWKHASSLK VANEPILAFT QGSPERDALQ
60 70 80 90 100
KALNDLKDQT EAIPCVVGDE EVWTSDVRYQ LSPFNHGHKV AKFCYADKAL
110 120 130 140 150
LNKAIEAAVL ARKEWDLKPV ADRAQIFLKA ADMLSGPRRA EILAKTMVGQ
160 170 180 190 200
GKTVIQAEID AAAELIDFFR FNAKFAVELE GEQPISVPPS TNHVVYRGLE
210 220 230 240 250
GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA SYAVYRILRE
260 270 280 290 300
AGLPPNVIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWKQVAQN
310 320 330 340 350
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC
360 370 380 390 400
SRLYVPQSLW PQIKGRLLEE HSRIKVGNPA EDFGTFFSAV IDAKAFARIK
410 420 430 440 450
KWLEHARSSP SLSILAGGQC NESVGYFVEP CIIESKDPQE PIMKEEIFGP
460 470 480 490 500
VLTVYVYPDE KYRETLQLVD STTSYGLTGA VFAQDKTIVQ EATRMLRNAA
510 520 530 540 550
GNFYINDKST GSVVGQQPFG GARASGERDI PGQPRLVQLW TEPPFTPLAV
560
SPPLGDWRYS YMQ
Length:563
Mass (Da):61,869
Last modified:May 15, 2007 - v1
Checksum:iAF19417D93825EA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03107656 Genomic DNA. No translation available.
UniGeneiRn.203318.

Genome annotation databases

UCSCiRGD:1624206. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03107656 Genomic DNA. No translation available.
UniGenei Rn.203318.

3D structure databases

ProteinModelPortali P0C2X9.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P0C2X9.
PRIDEi P0C2X9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1624206. rat.

Organism-specific databases

RGDi 1624206. Aldh4a1.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271511.
HOVERGENi HBG050484.
InParanoidi P0C2X9.
PhylomeDBi P0C2X9.

Enzyme and pathway databases

UniPathwayi UPA00261 ; UER00374 .
SABIO-RK P0C2X9.

Gene expression databases

Genevestigatori P0C2X9.

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.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01236. D1pyr5carbox1. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAL4A1_RAT
AccessioniPrimary (citable) accession number: P0C2X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: October 29, 2014
This is version 61 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3