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Q86XE5 (HOGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-2-oxoglutarate aldolase, mitochondrial

EC=4.1.3.16
Alternative name(s):
Dihydrodipicolinate synthase-like
Short name=DHDPS-like protein
Probable 2-keto-4-hydroxyglutarate aldolase
Short name=Probable KHG-aldolase
Protein 569272
Gene names
Name:HOGA1
Synonyms:C10orf65, DHDPSL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the final step in the metabolic pathway of hydroxyproline. Ref.6 Ref.7

Catalytic activity

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. Ref.7

Enzyme regulation

Inhibited by divalent cations By similarity.

Subunit structure

Homotetramer By similarity. Ref.7

Subcellular location

Mitochondrion By similarity.

Involvement in disease

Hyperoxaluria primary 3 (HP3) [MIM:613616]: A disorder phenotypically similar to hyperoxaluria type 1 and type 2. It is characterized by increase in urinary oxalate excretion and mild glycolic aciduria. Clinical manifestations include calcium oxalate urolithiasis, hematuria, pain, and/or urinary tract infection.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Belongs to the DapA family.

Sequence caution

The sequence CAC84901.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI15457.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86XE5-1)

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.
Isoform 2 (identifier: Q86XE5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     71-233: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion By similarity
Chain26 – 3273024-hydroxy-2-oxoglutarate aldolase, mitochondrial
PRO_0000273346

Regions

Region77 – 782Substrate binding

Sites

Active site1961Schiff-base intermediate with substrate Ref.7
Binding site1981Substrate
Binding site2221Substrate; via carbonyl oxygen
Site1681Involved in proton transfer during cleavage

Natural variations

Alternative sequence71 – 233163Missing in isoform 2.
VSP_022515
Natural variant2571C → G in HP3. Ref.6
VAR_064035
Natural variant2871G → V in HP3. Ref.6
VAR_064036
Natural variant3151Missing in HP3. Ref.6
VAR_064037

Experimental info

Mutagenesis771S → A: 2-fold decrease in Kcat and a nearly 8-fold increase in KM. Ref.7
Mutagenesis771S → T: Significant loss of activity. Ref.7
Mutagenesis781N → A: 6-fold increase in KM. Ref.7
Mutagenesis781N → Q: 25-fold increase in KM. Ref.7
Mutagenesis1401Y → F: No change in activity. Ref.7
Mutagenesis1681Y → F: No enzymatic activity. Ref.7
Mutagenesis1961K → A: No enzymatic activity. Ref.7
Mutagenesis1981S → A: 2.5-fold decrease in Kcat and 4.2 fold increase in KM. Ref.7
Mutagenesis1981S → T: 7-fold increase in KM. Ref.7

Secondary structure

.................................................. 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2DC011E4F9FD32C9

FASTA32735,249
        10         20         30         40         50         60 
MLGPQVWSSV RQGLSRSLSR NVGVWASGEG KKVDIAGIYP PVTTPFTATA EVDYGKLEEN 

        70         80         90        100        110        120 
LHKLGTFPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM PKNRLLLAGS GCESTQATVE 

       130        140        150        160        170        180 
MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPV 

       190        200        210        220        230        240 
DAVVTLSQHP NIVGMKDSGG DVTRIGLIVH KTRKQDFQVL AGSAGFLMAS YALGAVGGVC 

       250        260        270        280        290        300 
ALANVLGAQV CQLERLCCTG QWEDAQKLQH RLIEPNAAVT RRFGIPGLKK IMDWFGYYGG 

       310        320 
PCRAPLQELS PAEEEALRMD FTSNGWL 

« Hide

Isoform 2 [UniParc].

Checksum: 5DC5ADF3B9A891B4
Show »

FASTA16417,954

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Urinary bladder.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Hippocampus and Kidney.
[5]"Homo sapiens gene 569272."
Moschonas N.K.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-279 (ISOFORM 1).
[6]"Mutations in DHDPSL are responsible for primary hyperoxaluria type III."
Belostotsky R., Seboun E., Idelson G.H., Milliner D.S., Becker-Cohen R., Rinat C., Monico C.G., Feinstein S., Ben-Shalom E., Magen D., Weissman I., Charon C., Frishberg Y.
Am. J. Hum. Genet. 87:392-399(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANTS HP3 GLY-257; VAL-287 AND GLU-315 DEL.
[7]"Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria."
Riedel T.J., Johnson L.C., Knight J., Hantgan R.R., Holmes R.P., Lowther W.T.
PLoS ONE 6:E26021-E26021(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 26-327 IN COMPLEX WITH PYRUVATE, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-77; ASN-78; TYR-140; TYR-168; LYS-196 AND SER-198, FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK289440 mRNA. Translation: BAF82129.1.
AL355315 Genomic DNA. Translation: CAI15454.1.
AL355315 Genomic DNA. Translation: CAI15455.1.
AL355315 Genomic DNA. Translation: CAI15457.1. Sequence problems.
CH471066 Genomic DNA. Translation: EAW49912.1.
BC011916 mRNA. Translation: AAH11916.1.
BC045550 mRNA. Translation: AAH45550.1.
BC057821 mRNA. Translation: AAH57821.1.
AJ312051 Genomic DNA. Translation: CAC84901.1. Sequence problems.
RefSeqNP_001128142.1. NM_001134670.1.
NP_612422.2. NM_138413.3.
UniGeneHs.180346.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S5NX-ray2.50A26-327[»]
3S5OX-ray1.97A26-327[»]
ProteinModelPortalQ86XE5.
SMRQ86XE5. Positions 33-327.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ86XE5.
ChEMBLCHEMBL5996.

PTM databases

PhosphoSiteQ86XE5.

Polymorphism databases

DMDM74750531.

Proteomic databases

PaxDbQ86XE5.
PRIDEQ86XE5.

Protocols and materials databases

DNASU112817.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370646; ENSP00000359680; ENSG00000241935. [Q86XE5-1]
ENST00000370647; ENSP00000359681; ENSG00000241935. [Q86XE5-3]
GeneID112817.
KEGGhsa:112817.
UCSCuc001kny.3. human. [Q86XE5-1]
uc001knz.3. human. [Q86XE5-3]

Organism-specific databases

CTD112817.
GeneCardsGC10P099356.
HGNCHGNC:25155. HOGA1.
HPAHPA039466.
MIM613597. gene.
613616. phenotype.
neXtProtNX_Q86XE5.
Orphanet93600. Primary hyperoxaluria type 3.
PharmGKBPA165548441.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0329.
HOVERGENHBG081405.
InParanoidQ86XE5.
OMATHKEHMR.
PhylomeDBQ86XE5.
TreeFamTF324600.

Enzyme and pathway databases

BioCycMetaCyc:G66-31234-MONOMER.

Gene expression databases

BgeeQ86XE5.
CleanExHS_C10orf65.
GenevestigatorQ86XE5.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
PROSITEPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHOGA1. human.
GenomeRNAi112817.
NextBio78673.
PROQ86XE5.
SOURCESearch...

Entry information

Entry nameHOGA1_HUMAN
AccessionPrimary (citable) accession number: Q86XE5
Secondary accession number(s): A8K075 expand/collapse secondary AC list , Q5T680, Q5T684, Q711P0, Q8N9F2, Q96EV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM