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Protein

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

Gene

ALDH4A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.1 Publication

Kineticsi

  1. KM=100 µM for NAD1 Publication
  2. KM=32 µM for L-pyrroline-5-carboxylate1 Publication

    Pathwayi: L-proline degradation into L-glutamate

    This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Probable proline dehydrogenase 2 (PRODH2), 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 sitei208NADBy similarity1
    Sitei211Transition state stabilizerBy similarity1
    Binding sitei233NADBy similarity1
    Active sitei314Proton acceptorPROSITE-ProRule annotation1
    Active sitei348NucleophilePROSITE-ProRule annotation1 Publication1
    Binding sitei447NADBy similarity1
    Binding sitei513SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi286 – 290NADBy similarity5

    GO - Molecular functioni

    • 1-pyrroline-5-carboxylate dehydrogenase activity Source: Reactome
    • aldehyde dehydrogenase (NAD) activity Source: CACAO
    • electron carrier activity Source: UniProtKB

    GO - Biological processi

    • 4-hydroxyproline catabolic process Source: BHF-UCL
    • glutamate biosynthetic process Source: InterPro
    • proline biosynthetic process Source: InterPro
    • proline catabolic process Source: Reactome
    • proline catabolic process to glutamate Source: UniProtKB-UniPathway
    • proline metabolic process Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Proline metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS14757-MONOMER.
    ZFISH:HS14757-MONOMER.
    BRENDAi1.2.1.88. 2681.
    ReactomeiR-HSA-70688. Proline catabolism.
    SABIO-RKP30038.
    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
    Synonyms:ALDH4, P5CDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:406. ALDH4A1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Hyperprolinemia 2 (HYRPRO2)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn inborn error of proline metabolism resulting in elevated plasma levels of proline and delta-1-pyrroline-5-carboxylate (P5C). The condition is considered to be benign, but affected individuals can exhibit neurological manifestations that vary in severity. Clinical signs include seizures, intellectual deficit and mild developmental delay.
    See also OMIM:239510
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_002260352S → L in HYRPRO2; allele ALDH4A1*3; loss of enzyme activity. 2 PublicationsCorresponds to variant rs137852937dbSNPEnsembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi352S → A: Reduced affinity for NAD. No effect on enzyme activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi8659.
    MalaCardsiALDH4A1.
    MIMi239510. phenotype.
    OpenTargetsiENSG00000159423.
    Orphaneti79101. Hyperprolinemia type 2.
    PharmGKBiPA24701.

    Chemistry databases

    ChEMBLiCHEMBL3414418.

    Polymorphism and mutation databases

    BioMutaiALDH4A1.
    DMDMi62511241.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 24Mitochondrion1 PublicationAdd BLAST24
    ChainiPRO_000000717325 – 563Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialAdd BLAST539

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei31N6-succinyllysineBy similarity1
    Modified residuei44PhosphoserineCombined sources1
    Modified residuei52N6-acetyllysineBy similarity1
    Modified residuei93N6-acetyllysine; alternateBy similarity1
    Modified residuei93N6-succinyllysine; alternateBy similarity1
    Modified residuei99N6-acetyllysine; alternateBy similarity1
    Modified residuei99N6-succinyllysine; alternateBy similarity1
    Modified residuei114N6-acetyllysine; alternateBy similarity1
    Modified residuei114N6-succinyllysine; alternateBy similarity1
    Modified residuei130N6-acetyllysine; alternateBy similarity1
    Modified residuei130N6-succinyllysine; alternateBy similarity1
    Modified residuei175N6-acetyllysine; alternateBy similarity1
    Modified residuei175N6-succinyllysine; alternateBy similarity1
    Modified residuei318N6-acetyllysineBy similarity1
    Modified residuei347N6-succinyllysineBy similarity1
    Modified residuei365N6-acetyllysineBy similarity1
    Modified residuei376N6-acetyllysineBy similarity1
    Modified residuei395N6-succinyllysineBy similarity1
    Modified residuei462N6-acetyllysineBy similarity1
    Modified residuei509N6-acetyllysine; alternateBy similarity1
    Modified residuei509N6-succinyllysine; alternateBy similarity1
    Modified residuei531N6-acetyllysineBy similarity1
    Modified residuei552N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP30038.
    MaxQBiP30038.
    PaxDbiP30038.
    PeptideAtlasiP30038.
    PRIDEiP30038.

    2D gel databases

    OGPiP30038.
    SWISS-2DPAGEP30038.

    PTM databases

    iPTMnetiP30038.
    PhosphoSitePlusiP30038.

    Expressioni

    Tissue specificityi

    Highest expression is found in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas.

    Gene expression databases

    BgeeiENSG00000159423.
    CleanExiHS_ALDH4A1.
    ExpressionAtlasiP30038. baseline and differential.
    GenevisibleiP30038. HS.

    Organism-specific databases

    HPAiCAB004645.
    HPA006401.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-3926971,EBI-3926971

    Protein-protein interaction databases

    BioGridi114208. 23 interactors.
    IntActiP30038. 2 interactors.
    STRINGi9606.ENSP00000290597.

    Structurei

    Secondary structure

    1563
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi24 – 30Combined sources7
    Helixi45 – 57Combined sources13
    Beta strandi62 – 64Combined sources3
    Beta strandi66 – 68Combined sources3
    Beta strandi71 – 73Combined sources3
    Beta strandi78 – 83Combined sources6
    Beta strandi86 – 95Combined sources10
    Helixi99 – 118Combined sources20
    Helixi121 – 136Combined sources16
    Turni137 – 139Combined sources3
    Helixi140 – 151Combined sources12
    Helixi155 – 165Combined sources11
    Helixi167 – 180Combined sources14
    Beta strandi192 – 199Combined sources8
    Beta strandi201 – 207Combined sources7
    Helixi217 – 225Combined sources9
    Beta strandi229 – 233Combined sources5
    Helixi236 – 238Combined sources3
    Helixi239 – 251Combined sources13
    Beta strandi258 – 261Combined sources4
    Helixi266 – 274Combined sources9
    Beta strandi279 – 286Combined sources8
    Helixi288 – 300Combined sources13
    Helixi301 – 304Combined sources4
    Beta strandi310 – 315Combined sources6
    Beta strandi319 – 323Combined sources5
    Helixi329 – 341Combined sources13
    Helixi342 – 345Combined sources4
    Beta strandi351 – 357Combined sources7
    Turni358 – 360Combined sources3
    Helixi361 – 372Combined sources12
    Turni380 – 382Combined sources3
    Helixi394 – 409Combined sources16
    Beta strandi413 – 417Combined sources5
    Beta strandi424 – 426Combined sources3
    Beta strandi432 – 437Combined sources6
    Helixi442 – 445Combined sources4
    Beta strandi450 – 458Combined sources9
    Helixi460 – 462Combined sources3
    Helixi463 – 472Combined sources10
    Beta strandi475 – 477Combined sources3
    Beta strandi479 – 483Combined sources5
    Helixi487 – 496Combined sources10
    Turni497 – 500Combined sources4
    Beta strandi502 – 508Combined sources7
    Turni515 – 517Combined sources3
    Helixi528 – 530Combined sources3
    Beta strandi534 – 536Combined sources3
    Helixi537 – 541Combined sources5
    Beta strandi542 – 549Combined sources8
    Helixi560 – 562Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3V9GX-ray2.50A/B/C/D18-563[»]
    3V9HX-ray2.40A/B/C/D18-563[»]
    3V9IX-ray2.85A/B/C/D18-563[»]
    4OE5X-ray1.95A/B/C/D18-563[»]
    ProteinModelPortaliP30038.
    SMRiP30038.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG2455. Eukaryota.
    COG1012. LUCA.
    GeneTreeiENSGT00560000077335.
    HOVERGENiHBG050484.
    InParanoidiP30038.
    KOiK00294.
    OMAiKIWEKAA.
    OrthoDBiEOG091G085N.
    PhylomeDBiP30038.
    TreeFamiTF300481.

    Family and domain databases

    CDDicd07123. ALDH_F4-17_P5CDH. 1 hit.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P30038-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MLLPAPALRR ALLSRPWTGA GLRWKHTSSL KVANEPVLAF TQGSPERDAL
    60 70 80 90 100
    QKALKDLKGR MEAIPCVVGD EEVWTSDVQY QVSPFNHGHK VAKFCYADKS
    110 120 130 140 150
    LLNKAIEAAL AARKEWDLKP IADRAQIFLK AADMLSGPRR AEILAKTMVG
    160 170 180 190 200
    QGKTVIQAEI DAAAELIDFF RFNAKYAVEL EGQQPISVPP STNSTVYRGL
    210 220 230 240 250
    EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML ASYAVYRILR
    260 270 280 290 300
    EAGLPPNIIQ FVPADGPLFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ
    310 320 330 340 350
    NLDRFHTFPR LAGECGGKNF HFVHRSADVE SVVSGTLRSA FEYGGQKCSA
    360 370 380 390 400
    CSRLYVPHSL WPQIKGRLLE EHSRIKVGDP AEDFGTFFSA VIDAKSFARI
    410 420 430 440 450
    KKWLEHARSS PSLTILAGGK CDDSVGYFVE PCIVESKDPQ EPIMKEEIFG
    460 470 480 490 500
    PVLSVYVYPD DKYKETLQLV DSTTSYGLTG AVFSQDKDVV QEATKVLRNA
    510 520 530 540 550
    AGNFYINDKS TGSIVGQQPF GGARASGTND KPGGPHYILR WTSPQVIKET
    560
    HKPLGDWSYA YMQ
    Length:563
    Mass (Da):61,719
    Last modified:February 1, 2005 - v3
    Checksum:i4D964771B7DB5FFD
    GO
    Isoform 2 (identifier: P30038-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Show »
    Length:503
    Mass (Da):55,118
    Checksum:i51F7786045941395
    GO
    Isoform 3 (identifier: P30038-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         396-446: Missing.

    Show »
    Length:512
    Mass (Da):56,043
    Checksum:i1AA9C976895301FE
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti68V → M in AAC50501 (PubMed:8621661).Curated1
    Sequence conflicti68V → M in AAC50500 (PubMed:8621661).Curated1
    Sequence conflicti189 – 191PPS → LPY AA sequence (PubMed:8493898).Curated3
    Sequence conflicti189P → L AA sequence (PubMed:1395511).Curated1
    Sequence conflicti226M → I in BAD96206 (Ref. 4) Curated1
    Sequence conflicti271D → E AA sequence (PubMed:1395511).Curated1
    Sequence conflicti271D → E AA sequence (PubMed:8493898).Curated1
    Sequence conflicti354L → K AA sequence (PubMed:8493898).Curated1
    Sequence conflicti376K → R in BAD96206 (Ref. 4) Curated1
    Sequence conflicti524 – 526RAS → GSA AA sequence (PubMed:8493898).Curated3

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00225916P → L in allele ALDH4A1*4. 1 PublicationCorresponds to variant rs146450609dbSNPEnsembl.1
    Natural variantiVAR_002260352S → L in HYRPRO2; allele ALDH4A1*3; loss of enzyme activity. 2 PublicationsCorresponds to variant rs137852937dbSNPEnsembl.1
    Natural variantiVAR_029337470V → I.2 PublicationsCorresponds to variant rs2230709dbSNPEnsembl.1
    Natural variantiVAR_048903473T → A.Corresponds to variant rs6695033dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0437851 – 60Missing in isoform 2. 1 PublicationAdd BLAST60
    Alternative sequenceiVSP_047732396 – 446Missing in isoform 3. 1 PublicationAdd BLAST51

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U24267 mRNA. Translation: AAC50501.1.
    U24266 mRNA. Translation: AAC50500.1.
    FJ462711 mRNA. Translation: ACN89883.1.
    AK289972 mRNA. Translation: BAF82661.1.
    AK294552 mRNA. Translation: BAG57755.1.
    AK222486 mRNA. Translation: BAD96206.1.
    AL080251, AL954340 Genomic DNA. Translation: CAI23417.1.
    AL954340, AL080251 Genomic DNA. Translation: CAI39493.1.
    BX537160 Genomic DNA. No translation available.
    CH471134 Genomic DNA. Translation: EAW94858.1.
    BC007581 mRNA. Translation: AAH07581.1.
    BC023600 mRNA. Translation: AAH23600.1.
    CCDSiCCDS188.1. [P30038-1]
    CCDS53272.1. [P30038-2]
    CCDS81273.1. [P30038-3]
    RefSeqiNP_001154976.1. NM_001161504.1. [P30038-2]
    NP_001306147.1. NM_001319218.1. [P30038-3]
    NP_003739.2. NM_003748.3. [P30038-1]
    NP_733844.1. NM_170726.2. [P30038-1]
    UniGeneiHs.77448.

    Genome annotation databases

    EnsembliENST00000290597; ENSP00000290597; ENSG00000159423. [P30038-1]
    ENST00000375341; ENSP00000364490; ENSG00000159423. [P30038-1]
    ENST00000538309; ENSP00000442988; ENSG00000159423. [P30038-2]
    ENST00000538839; ENSP00000446071; ENSG00000159423. [P30038-3]
    GeneIDi8659.
    KEGGihsa:8659.
    UCSCiuc001bbb.4. human. [P30038-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U24267 mRNA. Translation: AAC50501.1.
    U24266 mRNA. Translation: AAC50500.1.
    FJ462711 mRNA. Translation: ACN89883.1.
    AK289972 mRNA. Translation: BAF82661.1.
    AK294552 mRNA. Translation: BAG57755.1.
    AK222486 mRNA. Translation: BAD96206.1.
    AL080251, AL954340 Genomic DNA. Translation: CAI23417.1.
    AL954340, AL080251 Genomic DNA. Translation: CAI39493.1.
    BX537160 Genomic DNA. No translation available.
    CH471134 Genomic DNA. Translation: EAW94858.1.
    BC007581 mRNA. Translation: AAH07581.1.
    BC023600 mRNA. Translation: AAH23600.1.
    CCDSiCCDS188.1. [P30038-1]
    CCDS53272.1. [P30038-2]
    CCDS81273.1. [P30038-3]
    RefSeqiNP_001154976.1. NM_001161504.1. [P30038-2]
    NP_001306147.1. NM_001319218.1. [P30038-3]
    NP_003739.2. NM_003748.3. [P30038-1]
    NP_733844.1. NM_170726.2. [P30038-1]
    UniGeneiHs.77448.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3V9GX-ray2.50A/B/C/D18-563[»]
    3V9HX-ray2.40A/B/C/D18-563[»]
    3V9IX-ray2.85A/B/C/D18-563[»]
    4OE5X-ray1.95A/B/C/D18-563[»]
    ProteinModelPortaliP30038.
    SMRiP30038.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114208. 23 interactors.
    IntActiP30038. 2 interactors.
    STRINGi9606.ENSP00000290597.

    Chemistry databases

    ChEMBLiCHEMBL3414418.

    PTM databases

    iPTMnetiP30038.
    PhosphoSitePlusiP30038.

    Polymorphism and mutation databases

    BioMutaiALDH4A1.
    DMDMi62511241.

    2D gel databases

    OGPiP30038.
    SWISS-2DPAGEP30038.

    Proteomic databases

    EPDiP30038.
    MaxQBiP30038.
    PaxDbiP30038.
    PeptideAtlasiP30038.
    PRIDEiP30038.

    Protocols and materials databases

    DNASUi8659.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000290597; ENSP00000290597; ENSG00000159423. [P30038-1]
    ENST00000375341; ENSP00000364490; ENSG00000159423. [P30038-1]
    ENST00000538309; ENSP00000442988; ENSG00000159423. [P30038-2]
    ENST00000538839; ENSP00000446071; ENSG00000159423. [P30038-3]
    GeneIDi8659.
    KEGGihsa:8659.
    UCSCiuc001bbb.4. human. [P30038-1]

    Organism-specific databases

    CTDi8659.
    DisGeNETi8659.
    GeneCardsiALDH4A1.
    HGNCiHGNC:406. ALDH4A1.
    HPAiCAB004645.
    HPA006401.
    MalaCardsiALDH4A1.
    MIMi239510. phenotype.
    606811. gene.
    neXtProtiNX_P30038.
    OpenTargetsiENSG00000159423.
    Orphaneti79101. Hyperprolinemia type 2.
    PharmGKBiPA24701.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2455. Eukaryota.
    COG1012. LUCA.
    GeneTreeiENSGT00560000077335.
    HOVERGENiHBG050484.
    InParanoidiP30038.
    KOiK00294.
    OMAiKIWEKAA.
    OrthoDBiEOG091G085N.
    PhylomeDBiP30038.
    TreeFamiTF300481.

    Enzyme and pathway databases

    UniPathwayiUPA00261; UER00374.
    BioCyciMetaCyc:HS14757-MONOMER.
    ZFISH:HS14757-MONOMER.
    BRENDAi1.2.1.88. 2681.
    ReactomeiR-HSA-70688. Proline catabolism.
    SABIO-RKP30038.

    Miscellaneous databases

    ChiTaRSiALDH4A1. human.
    GeneWikiiAldehyde_dehydrogenase_4_family,_member_A1.
    GenomeRNAii8659.
    PROiP30038.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000159423.
    CleanExiHS_ALDH4A1.
    ExpressionAtlasiP30038. baseline and differential.
    GenevisibleiP30038. HS.

    Family and domain databases

    CDDicd07123. ALDH_F4-17_P5CDH. 1 hit.
    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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAL4A1_HUMAN
    AccessioniPrimary (citable) accession number: P30038
    Secondary accession number(s): A8K1Q7
    , B4DGE4, D2D4A3, Q16882, Q53HU4, Q5JNV6, Q8IZ38, Q96IF0, Q9UDI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 2005
    Last modified: November 2, 2016
    This is version 178 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.