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HUMAN:AL4A1
Contents
| Species (Taxon ID) | Homo sapiens (Human). (9606) | |
| Gene Name(s) | ALDH4A1 (synonyms: ALDH4, P5CDH) | |
| Protein Name(s) | Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
P5C dehydrogenase Aldehyde dehydrogenase family 4 member A1 L-glutamate gamma-semialdehyde dehydrogenase | |
| External Links | ||
| UniProt | P30038 | |
| EMBL | U24267 U24266 FJ462711 AK289972 AK294552 AK222486 AL080251 AL954340 AL954340 AL080251 BX537160 CH471134 BC007581 BC023600 | |
| CCDS | CCDS188.1 CCDS53272.1 | |
| RefSeq | NP_001154976.1 NP_003739.2 NP_733844.1 | |
| UniGene | Hs.77448 | |
| PDB | 3V9G 3V9H 3V9I 4OE5 | |
| PDBsum | 3V9G 3V9H 3V9I 4OE5 | |
| ProteinModelPortal | P30038 | |
| SMR | P30038 | |
| BioGrid | 114208 | |
| IntAct | P30038 | |
| STRING | 9606.ENSP00000290597 | |
| PhosphoSite | P30038 | |
| DMDM | 62511241 | |
| OGP | P30038 | |
| SWISS-2DPAGE | P30038 | |
| MaxQB | P30038 | |
| PaxDb | P30038 | |
| PRIDE | P30038 | |
| DNASU | 8659 | |
| Ensembl | ENST00000290597 ENST00000375341 ENST00000538309 ENST00000538839 | |
| GeneID | 8659 | |
| KEGG | hsa:8659 | |
| UCSC | uc001bbb.3 uc021ohl.1 | |
| CTD | 8659 | |
| GeneCards | GC01M019197 | |
| HGNC | HGNC:406 | |
| HPA | CAB004645 HPA006401 | |
| MIM | 239510 606811 | |
| neXtProt | NX_P30038 | |
| Orphanet | 79101 | |
| PharmGKB | PA24701 | |
| eggNOG | COG1012 | |
| GeneTree | ENSGT00560000077335 | |
| HOVERGEN | HBG050484 | |
| InParanoid | P30038 | |
| KO | K00294 | |
| OMA | LTDWKYP | |
| OrthoDB | EOG7T1R9D | |
| PhylomeDB | P30038 | |
| TreeFam | TF300481 | |
| BioCyc | MetaCyc:HS14757-MONOMER | |
| Reactome | REACT_1002 | |
| SABIO-RK | P30038 | |
| UniPathway | UPA00261 | |
| ChiTaRS | ALDH4A1 | |
| GeneWiki | Aldehyde_dehydrogenase_4_family,_member_A1 | |
| GenomeRNAi | 8659 | |
| NextBio | 32473 | |
| PRO | PR:P30038 | |
| Proteomes | UP000005640 | |
| Bgee | P30038 | |
| CleanEx | HS_ALDH4A1 | |
| ExpressionAtlas | P30038 | |
| Genevestigator | P30038 | |
| GO | GO:0005759 GO:0003842 GO:0004029 GO:0009055 GO:0042802 GO:0019470 GO:0034641 GO:0006537 GO:0006561 GO:0006562 GO:0010133 GO:0006560 GO:0044281 | |
| Gene3D | 3.40.309.10 3.40.605.10 | |
| InterPro | IPR016161 IPR016163 IPR016160 IPR029510 IPR016162 IPR015590 IPR005931 | |
| Pfam | PF00171 | |
| SUPFAM | SSF53720 | |
| TIGRFAMs | TIGR01236 | |
| PROSITE | PS00070 PS00687 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004029 |
aldehyde dehydrogenase (NAD) activity |
ECO:0000314 |
F |
Table 1, The gels were stained for ALDH activity with an agar overlay containing propionaldehyde or benzaldehyde |
complete | |||||
|
enables |
GO:0004029 |
aldehyde dehydrogenase (NAD) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003842 |
1-pyrroline-5-carboxylate dehydrogenase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:2443883 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0022900 |
electron transport chain |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0009055 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003842 |
1-pyrroline-5-carboxylate dehydrogenase activity |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:Q8CHT0 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003842 |
1-pyrroline-5-carboxylate dehydrogenase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0010133 |
proline catabolic process to glutamate |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR015590 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016620 |
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR015590 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006562 |
proline catabolic process |
PMID:8621661[4] |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
P |
Seeded From UniProt |
complete | |
|
involved_in |
GO:0006560 |
proline metabolic process |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005759 |
mitochondrial matrix |
PMID:8621661[4] |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
|
enables |
GO:0004029 |
aldehyde dehydrogenase (NAD) activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003842 |
1-pyrroline-5-carboxylate dehydrogenase activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019470 |
4-hydroxyproline catabolic process |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0009055 |
electron transfer activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046487 |
glyoxylate metabolic process |
Reactome:R-HSA-6784399 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006560 |
proline metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005759 |
mitochondrial matrix |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0010133 |
proline catabolic process to glutamate |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00261 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Hopkinson, DA et al. () Biochemical genetic analysis of human and rodent aldehyde dehydrogenase (ALDH). Alcohol 2 73-8 PubMed GONUTS page
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Srivastava, D et al. (2012) The three-dimensional structural basis of type II hyperprolinemia. J. Mol. Biol. 420 176-89 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Hu, CA et al. (1996) Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J. Biol. Chem. 271 9795-800 PubMed GONUTS page
- ↑ Riedel, TJ et al. (2011) Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria. PLoS ONE 6 e26021 PubMed GONUTS page
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