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Q9DCU9 (HOGA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:Hoga1
Synonyms:Dhdpsl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the final step in the metabolic pathway of hydroxyproline By similarity.

Catalytic activity

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

Enzyme regulation

Inhibited by divalent cations By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the DapA family.

Sequence caution

The sequence AAH16430.1 differs from that shown. Reason: Erroneous termination at position 322. Translated as stop.

The sequence BAB27226.1 differs from that shown. Reason: Frameshift at position 270.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion By similarity
Chain24 – 3212984-hydroxy-2-oxoglutarate aldolase, mitochondrial
PRO_0000273347

Regions

Region71 – 722Substrate binding By similarity

Sites

Active site1901Schiff-base intermediate with substrate By similarity
Binding site1921Substrate By similarity
Binding site2161Substrate; via carbonyl oxygen By similarity
Site1621Involved in proton transfer during cleavage By similarity

Experimental info

Sequence conflict251K → M in BAB27226. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DCU9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 75B3DC959756D5A7

FASTA32134,644
        10         20         30         40         50         60 
MLGPQIWASM RQGLSRGLSR NVKGKKVDIA GIYPPVTTPF TATAEVDYGK LEENLNRLAT 

        70         80         90        100        110        120 
FPFRGFVVQG STGEFPFLTS LERLEVVSRV RQAIPKDKFL IAGSGCESTQ ATVEMTVSMA 

       130        140        150        160        170        180 
QVGADVAMVV TPCYYRGRMS SAALIHHYTK VADVSPIPVV LYSVPANTGL ELPVDAVVTL 

       190        200        210        220        230        240 
SQHPNIIGLK DSGGDVTRIG LIVHKTSKQD FQVLAGSAGF LLASYAVGAV GGICGLANVL 

       250        260        270        280        290        300 
GAQVCQLERL CLTGQWEAAQ ELQHRLIEPN TAVTRRFGIP GLKKTMDWFG YYGGPCRAPL 

       310        320 
QELSPTEEEA LRLDFSNNGW L 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney and Liver.
[2]"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].
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002457 mRNA. Translation: BAB22114.1.
AK010857 mRNA. Translation: BAB27226.1. Frameshift.
BC016430 mRNA. Translation: AAH16430.1. Sequence problems.
CCDSCCDS29820.1.
RefSeqNP_080428.1. NM_026152.1.
UniGeneMm.24196.

3D structure databases

ProteinModelPortalQ9DCU9.
SMRQ9DCU9. Positions 27-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DCU9. 2 interactions.
MINTMINT-1860303.

PTM databases

PhosphoSiteQ9DCU9.

Proteomic databases

MaxQBQ9DCU9.
PaxDbQ9DCU9.
PRIDEQ9DCU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081714; ENSMUSP00000080414; ENSMUSG00000025176.
GeneID67432.
KEGGmmu:67432.
UCSCuc008hnb.1. mouse.

Organism-specific databases

CTD112817.
MGIMGI:1914682. Hoga1.

Phylogenomic databases

eggNOGCOG0329.
GeneTreeENSGT00530000063604.
HOVERGENHBG081405.
InParanoidQ9DCU9.
KOK18123.
OMALADHENI.
PhylomeDBQ9DCU9.
TreeFamTF324600.

Gene expression databases

ArrayExpressQ9DCU9.
BgeeQ9DCU9.
CleanExMM_0610010D20RIK.
GenevestigatorQ9DCU9.

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. mouse.
NextBio324548.
PROQ9DCU9.
SOURCESearch...

Entry information

Entry nameHOGA1_MOUSE
AccessionPrimary (citable) accession number: Q9DCU9
Secondary accession number(s): Q91W74, Q9CY60
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot