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Protein

Serine--pyruvate aminotransferase, mitochondrial

Gene

Agxt

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

Functioni

Dual metabolic roles of gluconeogenesis (in the mitochondria) and glyoxylate detoxification (in the peroxisomes).By similarity

Catalytic activityi

L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.
L-alanine + glyoxylate = pyruvate + glycine.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei382 – 3821SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
SABIO-RKO35423.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--pyruvate aminotransferase, mitochondrial (EC:2.6.1.51)
Short name:
SPT
Alternative name(s):
Alanine--glyoxylate aminotransferase (EC:2.6.1.44)
Short name:
AGT
Gene namesi
Name:Agxt
Synonyms:Agxt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1329033. Agxt.

Subcellular locationi

  • Mitochondrion matrix By similarity
  • Peroxisome By similarity

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: HGNC
  • peroxisomal matrix Source: MGI
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionAdd
BLAST
Chaini25 – 414390Serine--pyruvate aminotransferase, mitochondrialPRO_0000001288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei247 – 2471N6-acetyllysine; alternateCombined sources
Modified residuei247 – 2471N6-succinyllysine; alternateCombined sources
Modified residuei256 – 2561N6-acetyllysineCombined sources
Modified residuei330 – 3301N6-acetyllysine; alternateCombined sources
Modified residuei330 – 3301N6-succinyllysine; alternateCombined sources
Modified residuei334 – 3341N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO35423.
PaxDbiO35423.
PRIDEiO35423.

PTM databases

iPTMnetiO35423.
PhosphoSiteiO35423.
SwissPalmiO35423.

Expressioni

Gene expression databases

CleanExiMM_AGXT.
GenevisibleiO35423. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiO35423. 2 interactions.
MINTiMINT-1859331.
STRINGi10090.ENSMUSP00000027491.

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 374Combined sources
Beta strandi49 – 513Combined sources
Helixi57 – 626Combined sources
Helixi73 – 9018Combined sources
Beta strandi95 – 1017Combined sources
Turni104 – 1063Combined sources
Helixi107 – 1159Combined sources
Beta strandi121 – 1288Combined sources
Helixi129 – 14012Combined sources
Beta strandi144 – 1496Combined sources
Helixi158 – 16811Combined sources
Beta strandi171 – 1799Combined sources
Turni180 – 1834Combined sources
Helixi191 – 1977Combined sources
Beta strandi201 – 2055Combined sources
Turni207 – 2126Combined sources
Turni217 – 2215Combined sources
Beta strandi224 – 2318Combined sources
Beta strandi240 – 2445Combined sources
Helixi246 – 2538Combined sources
Helixi266 – 2727Combined sources
Beta strandi276 – 2783Combined sources
Helixi288 – 30417Combined sources
Helixi306 – 32621Combined sources
Beta strandi331 – 3355Combined sources
Helixi336 – 3383Combined sources
Beta strandi341 – 3477Combined sources
Helixi354 – 36512Combined sources
Helixi374 – 3763Combined sources
Turni377 – 3793Combined sources
Beta strandi380 – 3845Combined sources
Helixi387 – 3893Combined sources
Helixi392 – 40817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KGWX-ray1.65A/B23-414[»]
3KGXX-ray1.80A/B23-414[»]
ProteinModelPortaliO35423.
SMRiO35423. Positions 27-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35423.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi412 – 4143Microbody targeting signalBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2862. Eukaryota.
COG0075. LUCA.
GeneTreeiENSGT00390000006648.
HOGENOMiHOG000171815.
HOVERGENiHBG006907.
InParanoidiO35423.
KOiK00830.
OMAiAYSCSQK.
OrthoDBiEOG7CZK6B.
TreeFamiTF313234.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR024169. SP_NH2Trfase/AEP_transaminase.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000524. SPT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: O35423-1) [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
MFRMLAKASV TLGSRAAGWV RTMGSYQLLV PPPEALSKPL SVPTRLLLGP
60 70 80 90 100
GPSNLAPRVL AAGSLRMIGH MQKEMLQIME EIKQGIQYVF QTRNPLTLVV
110 120 130 140 150
SGSGHCAMET ALFNLLEPGD SFLTGTNGIW GMRAAEIADR IGARVHQMIK
160 170 180 190 200
KPGEHYTLQE VEEGLAQHKP VLLFLVHGES STGVVQPLDG FGELCHRYQC
210 220 230 240 250
LLLVDSVASL GGVPIYMDQQ GIDIMYSSSQ KVLNAPPGIS LISFNDKAKY
260 270 280 290 300
KVYSRKTKPV SFYTDITYLA KLWGCEGETR VIHHTTPVTS LYCLRESLAL
310 320 330 340 350
IAEQGLENCW RRHREATAHL HKHLQEMGLK FFVKDPEIRL PTITTVTVPA
360 370 380 390 400
GYNWRDIVSY VLDHFSIEIS GGLGPTEERV LRIGLLGYNA TTENVDRVAE
410
ALREALQHCP KNKL
Length:414
Mass (Da):45,912
Last modified:April 3, 2013 - v3
Checksum:iA2AB28AC48A292E3
GO
Isoform Peroxisomal (identifier: O35423-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.

Show »
Length:392
Mass (Da):43,520
Checksum:iD7452F1A576BCA17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041Q → R in AAB82001 (PubMed:11225057).Curated
Sequence conflicti348 – 3492VP → A in AAB82001 (PubMed:11225057).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222Missing in isoform Peroxisomal. 1 PublicationVSP_018644Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027730 mRNA. Translation: AAB82001.2.
AC110247 Genomic DNA. No translation available.
CH466520 Genomic DNA. Translation: EDL39972.1.
BC025799 mRNA. Translation: AAH25799.1.
CCDSiCCDS15184.1. [O35423-1]
RefSeqiNP_057911.2. NM_016702.3. [O35423-1]
UniGeneiMm.7457.

Genome annotation databases

EnsembliENSMUST00000027491; ENSMUSP00000027491; ENSMUSG00000026272. [O35423-1]
GeneIDi11611.
KEGGimmu:11611.
UCSCiuc007cdi.2. mouse. [O35423-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027730 mRNA. Translation: AAB82001.2.
AC110247 Genomic DNA. No translation available.
CH466520 Genomic DNA. Translation: EDL39972.1.
BC025799 mRNA. Translation: AAH25799.1.
CCDSiCCDS15184.1. [O35423-1]
RefSeqiNP_057911.2. NM_016702.3. [O35423-1]
UniGeneiMm.7457.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KGWX-ray1.65A/B23-414[»]
3KGXX-ray1.80A/B23-414[»]
ProteinModelPortaliO35423.
SMRiO35423. Positions 27-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35423. 2 interactions.
MINTiMINT-1859331.
STRINGi10090.ENSMUSP00000027491.

PTM databases

iPTMnetiO35423.
PhosphoSiteiO35423.
SwissPalmiO35423.

Proteomic databases

EPDiO35423.
PaxDbiO35423.
PRIDEiO35423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027491; ENSMUSP00000027491; ENSMUSG00000026272. [O35423-1]
GeneIDi11611.
KEGGimmu:11611.
UCSCiuc007cdi.2. mouse. [O35423-1]

Organism-specific databases

CTDi189.
MGIiMGI:1329033. Agxt.

Phylogenomic databases

eggNOGiKOG2862. Eukaryota.
COG0075. LUCA.
GeneTreeiENSGT00390000006648.
HOGENOMiHOG000171815.
HOVERGENiHBG006907.
InParanoidiO35423.
KOiK00830.
OMAiAYSCSQK.
OrthoDBiEOG7CZK6B.
TreeFamiTF313234.

Enzyme and pathway databases

ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
SABIO-RKO35423.

Miscellaneous databases

ChiTaRSiAgxt. mouse.
EvolutionaryTraceiO35423.
PROiO35423.
SOURCEiSearch...

Gene expression databases

CleanExiMM_AGXT.
GenevisibleiO35423. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR024169. SP_NH2Trfase/AEP_transaminase.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000524. SPT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse alanine:glyoxylate aminotransferase gene (Agxt1): cloning, expression, and mapping to chromosome 1."
    Li X.M., Salido E.C., Shapiro L.J.
    Somat. Cell Mol. Genet. 25:67-77(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MITOCHONDRIAL AND PEROXISOMAL).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., 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] (ISOFORM MITOCHONDRIAL).
    Strain: FVB/N.
    Tissue: Liver.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-247 AND LYS-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247; LYS-256; LYS-330 AND LYS-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Crystal structure of putative aminotransferase (AAH25799.1) from Mus musculus at 1.65 A resolution."
    Joint center for structural genomics (JCSG)
    Submitted (OCT-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 23-414.

Entry informationi

Entry nameiSPYA_MOUSE
AccessioniPrimary (citable) accession number: O35423
Secondary accession number(s): Q8R128
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 3, 2013
Last modified: June 8, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.