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Protein

4-hydroxy-2-oxoglutarate aldolase, mitochondrial

Gene

Hoga1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Inhibited by divalent cations.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei162 – 1621Involved in proton transfer during cleavageBy similarity
Active sitei190 – 1901Schiff-base intermediate with substrateBy similarity
Binding sitei192 – 1921SubstrateBy similarity
Binding sitei216 – 2161Substrate; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Schiff base

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Hoga1
Synonyms:Dhdpsl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1914682. Hoga1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 3212984-hydroxy-2-oxoglutarate aldolase, mitochondrialPRO_0000273347Add
BLAST

Proteomic databases

MaxQBiQ9DCU9.
PaxDbiQ9DCU9.
PRIDEiQ9DCU9.

PTM databases

PhosphoSiteiQ9DCU9.

Expressioni

Gene expression databases

BgeeiQ9DCU9.
CleanExiMM_0610010D20RIK.
ExpressionAtlasiQ9DCU9. baseline and differential.
GenevestigatoriQ9DCU9.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9DCU9. 2 interactions.
MINTiMINT-1860303.

Structurei

3D structure databases

ProteinModelPortaliQ9DCU9.
SMRiQ9DCU9. Positions 27-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 722Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the DapA family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0329.
GeneTreeiENSGT00530000063604.
HOVERGENiHBG081405.
InParanoidiQ9DCU9.
KOiK18123.
OMAiGFLMAAY.
PhylomeDBiQ9DCU9.
TreeFamiTF324600.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Schiff_base-form_aldolases_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DCU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGPQIWASM RQGLSRGLSR NVKGKKVDIA GIYPPVTTPF TATAEVDYGK
60 70 80 90 100
LEENLNRLAT FPFRGFVVQG STGEFPFLTS LERLEVVSRV RQAIPKDKFL
110 120 130 140 150
IAGSGCESTQ ATVEMTVSMA QVGADVAMVV TPCYYRGRMS SAALIHHYTK
160 170 180 190 200
VADVSPIPVV LYSVPANTGL ELPVDAVVTL SQHPNIIGLK DSGGDVTRIG
210 220 230 240 250
LIVHKTSKQD FQVLAGSAGF LLASYAVGAV GGICGLANVL GAQVCQLERL
260 270 280 290 300
CLTGQWEAAQ ELQHRLIEPN TAVTRRFGIP GLKKTMDWFG YYGGPCRAPL
310 320
QELSPTEEEA LRLDFSNNGW L
Length:321
Mass (Da):34,644
Last modified:June 1, 2001 - v1
Checksum:i75B3DC959756D5A7
GO

Sequence cautioni

The sequence AAH16430.1 differs from that shown. Reason: Erroneous termination at position 322. Translated as stop.Curated
The sequence BAB27226.1 differs from that shown. Reason: Frameshift at position 270. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251K → M in BAB27226 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002457 mRNA. Translation: BAB22114.1.
AK010857 mRNA. Translation: BAB27226.1. Frameshift.
BC016430 mRNA. Translation: AAH16430.1. Sequence problems.
CCDSiCCDS29820.1.
RefSeqiNP_080428.1. NM_026152.1.
UniGeneiMm.24196.

Genome annotation databases

EnsembliENSMUST00000081714; ENSMUSP00000080414; ENSMUSG00000025176.
GeneIDi67432.
KEGGimmu:67432.
UCSCiuc008hnb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002457 mRNA. Translation: BAB22114.1.
AK010857 mRNA. Translation: BAB27226.1. Frameshift.
BC016430 mRNA. Translation: AAH16430.1. Sequence problems.
CCDSiCCDS29820.1.
RefSeqiNP_080428.1. NM_026152.1.
UniGeneiMm.24196.

3D structure databases

ProteinModelPortaliQ9DCU9.
SMRiQ9DCU9. Positions 27-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DCU9. 2 interactions.
MINTiMINT-1860303.

PTM databases

PhosphoSiteiQ9DCU9.

Proteomic databases

MaxQBiQ9DCU9.
PaxDbiQ9DCU9.
PRIDEiQ9DCU9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081714; ENSMUSP00000080414; ENSMUSG00000025176.
GeneIDi67432.
KEGGimmu:67432.
UCSCiuc008hnb.1. mouse.

Organism-specific databases

CTDi112817.
MGIiMGI:1914682. Hoga1.

Phylogenomic databases

eggNOGiCOG0329.
GeneTreeiENSGT00530000063604.
HOVERGENiHBG081405.
InParanoidiQ9DCU9.
KOiK18123.
OMAiGFLMAAY.
PhylomeDBiQ9DCU9.
TreeFamiTF324600.

Miscellaneous databases

ChiTaRSiHoga1. mouse.
NextBioi324548.
PROiQ9DCU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCU9.
CleanExiMM_0610010D20RIK.
ExpressionAtlasiQ9DCU9. baseline and differential.
GenevestigatoriQ9DCU9.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Schiff_base-form_aldolases_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiHOGA1_MOUSE
AccessioniPrimary (citable) accession number: Q9DCU9
Secondary accession number(s): Q91W74, Q9CY60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2001
Last modified: May 27, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.