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Protein

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

Gene

Aldh4a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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: L-proline degradation into L-glutamate

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Proline dehydrogenase 1, mitochondrial (Prodh)
  2. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (Aldh4a1)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei207NAD1
Sitei210Transition state stabilizerBy similarity1
Binding sitei232NAD1
Active sitei313Proton acceptorPROSITE-ProRule annotation1 Publication1
Active sitei347NucleophilePROSITE-ProRule annotation1 Publication1
Binding sitei446NAD1
Binding sitei512Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi285 – 289NAD5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processProline metabolism
LigandNAD

Enzyme and pathway databases

ReactomeiR-MMU-389661 Glyoxylate metabolism and glycine degradation
R-MMU-70688 Proline catabolism
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2443883 Aldh4a1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 23MitochondrionBy similarityAdd BLAST23
ChainiPRO_000000717424 – 562Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialAdd BLAST539

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30N6-succinyllysineCombined sources1
Modified residuei43PhosphoserineBy similarity1
Modified residuei51N6-acetyllysineCombined sources1
Modified residuei92N6-acetyllysine; alternateCombined sources1
Modified residuei92N6-succinyllysine; alternateCombined sources1
Modified residuei98N6-acetyllysine; alternateCombined sources1
Modified residuei98N6-succinyllysine; alternateCombined sources1
Modified residuei113N6-acetyllysine; alternateCombined sources1
Modified residuei113N6-succinyllysine; alternateCombined sources1
Modified residuei129N6-acetyllysine; alternateCombined sources1
Modified residuei129N6-succinyllysine; alternateCombined sources1
Modified residuei174N6-acetyllysine; alternateCombined sources1
Modified residuei174N6-succinyllysine; alternateCombined sources1
Modified residuei317N6-acetyllysineCombined sources1
Modified residuei346N6-succinyllysineCombined sources1
Modified residuei357N6-acetyllysine; alternateCombined sources1
Modified residuei357N6-succinyllysine; alternateCombined sources1
Modified residuei364N6-acetyllysineCombined sources1
Modified residuei375N6-acetyllysineCombined sources1
Modified residuei394N6-succinyllysineCombined sources1
Modified residuei461N6-acetyllysineCombined sources1
Modified residuei508N6-acetyllysine; alternateCombined sources1
Modified residuei508N6-succinyllysine; alternateCombined sources1
Modified residuei530N6-acetyllysineCombined sources1
Modified residuei551N6-acetyllysineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CHT0
MaxQBiQ8CHT0
PaxDbiQ8CHT0
PeptideAtlasiQ8CHT0
PRIDEiQ8CHT0

PTM databases

iPTMnetiQ8CHT0
PhosphoSitePlusiQ8CHT0
SwissPalmiQ8CHT0

Expressioni

Gene expression databases

BgeeiENSMUSG00000028737
CleanExiMM_ALDH4A1
GenevisibleiQ8CHT0 MM

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229346, 2 interactors
IntActiQ8CHT0, 6 interactors
MINTiQ8CHT0
STRINGi10090.ENSMUSP00000043821

Structurei

Secondary structure

1562
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 54Combined sources11
Turni55 – 58Combined sources4
Beta strandi65 – 67Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi77 – 82Combined sources6
Beta strandi85 – 94Combined sources10
Helixi98 – 117Combined sources20
Helixi120 – 135Combined sources16
Turni136 – 138Combined sources3
Helixi139 – 150Combined sources12
Helixi154 – 160Combined sources7
Helixi163 – 179Combined sources17
Beta strandi190 – 195Combined sources6
Beta strandi200 – 206Combined sources7
Helixi212 – 224Combined sources13
Beta strandi229 – 232Combined sources4
Helixi235 – 237Combined sources3
Helixi238 – 250Combined sources13
Beta strandi257 – 260Combined sources4
Helixi265 – 272Combined sources8
Beta strandi278 – 285Combined sources8
Helixi287 – 299Combined sources13
Turni300 – 303Combined sources4
Beta strandi309 – 313Combined sources5
Beta strandi318 – 322Combined sources5
Helixi328 – 340Combined sources13
Helixi341 – 344Combined sources4
Beta strandi350 – 356Combined sources7
Helixi357 – 359Combined sources3
Helixi360 – 372Combined sources13
Turni379 – 381Combined sources3
Helixi393 – 408Combined sources16
Beta strandi412 – 416Combined sources5
Beta strandi423 – 425Combined sources3
Beta strandi431 – 436Combined sources6
Helixi441 – 443Combined sources3
Beta strandi449 – 457Combined sources9
Helixi459 – 461Combined sources3
Helixi462 – 471Combined sources10
Beta strandi472 – 482Combined sources11
Helixi486 – 495Combined sources10
Turni496 – 499Combined sources4
Beta strandi501 – 507Combined sources7
Turni514 – 516Combined sources3
Helixi536 – 540Combined sources5
Beta strandi544 – 549Combined sources6
Helixi559 – 561Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ8CHT0
SMRiQ8CHT0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2455 Eukaryota
COG1012 LUCA
GeneTreeiENSGT00560000077335
HOGENOMiHOG000271511
HOVERGENiHBG050484
InParanoidiQ8CHT0
KOiK00294
OMAiPHYVLRW
OrthoDBiEOG091G085N
TreeFamiTF300481

Family and domain databases

CDDicd07123 ALDH_F4-17_P5CDH, 1 hit
Gene3Di3.40.309.10, 1 hit
3.40.605.10, 2 hits
InterProiView protein in InterPro
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
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
TIGRFAMsiTIGR01236 D1pyr5carbox1, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q8CHT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ
60 70 80 90 100
KALKDLKGQM EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL
110 120 130 140 150
LNRAIDAALA ARKEWDLKPM ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ
160 170 180 190 200
GKTVIQAEID AAAELIDFFR FNAKFAVELE GEQPISVPPS TNHTVYRGLE
210 220 230 240 250
GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA SYAVYRILRE
260 270 280 290 300
AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN
310 320 330 340 350
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC
360 370 380 390 400
SRLYVPKSLW PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK
410 420 430 440 450
KWLEHARSSP SLSILAGGQC NESVGYYVEP CIIESKDPQE PIMKEEIFGP
460 470 480 490 500
VLTVYVYPDD KYRETLQLVD STTSYGLTGA VFAQDKAIVQ EATRMLRNAA
510 520 530 540 550
GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW TSPQVIKETH
560
KPLGDWRYSY MQ
Length:562
Mass (Da):61,841
Last modified:July 27, 2011 - v3
Checksum:i4D8A0C9C68A99478
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18G → S in BAC32045 (PubMed:16141072).Curated1
Sequence conflicti18G → S in AAH56226 (PubMed:15489334).Curated1
Sequence conflicti18G → S in AAH39281 (PubMed:15489334).Curated1
Sequence conflicti18G → S in AAH24133 (PubMed:15489334).Curated1
Sequence conflicti32T → A in BAC32045 (PubMed:16141072).Curated1
Sequence conflicti32T → A in AAH56226 (PubMed:15489334).Curated1
Sequence conflicti32T → A in AAH39281 (PubMed:15489334).Curated1
Sequence conflicti32T → A in AAH24133 (PubMed:15489334).Curated1
Sequence conflicti47D → G in BAC32045 (PubMed:16141072).Curated1
Sequence conflicti60M → T in BAC32045 (PubMed:16141072).Curated1
Sequence conflicti60M → T in AAH56226 (PubMed:15489334).Curated1
Sequence conflicti60M → T in AAH39281 (PubMed:15489334).Curated1
Sequence conflicti60M → T in AAH24133 (PubMed:15489334).Curated1
Sequence conflicti467Q → K in BAC32045 (PubMed:16141072).Curated1
Sequence conflicti467Q → K in AAH56226 (PubMed:15489334).Curated1
Sequence conflicti467Q → K in AAH39281 (PubMed:15489334).Curated1
Sequence conflicti467Q → K in AAH24133 (PubMed:15489334).Curated1
Sequence conflicti467Q → K in AAH26589 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS18848.1
RefSeqiNP_780647.3, NM_175438.4
UniGeneiMm.273571

Genome annotation databases

EnsembliENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737
GeneIDi212647
KEGGimmu:212647
UCSCiuc012dnu.1 mouse

Similar proteinsi

Entry informationi

Entry nameiAL4A1_MOUSE
AccessioniPrimary (citable) accession number: Q8CHT0
Secondary accession number(s): B1AXW8
, Q7TND0, Q8BXM3, Q8R0N1, Q8R1S2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 141 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health