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Protein

Kynurenine--oxoglutarate transaminase 1

Gene

Ccbl1

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

Functioni

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity).By similarity

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine.
An L-cysteine-S-conjugate + H2O = RSH + NH3 + pyruvate.

Cofactori

Pathwayi: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes kynurenate from L-kynurenine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Kynurenine--oxoglutarate transaminase 1 (Ccbl1)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-kynurenine degradation, 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 kynurenate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate; via amide nitrogenBy similarity
Binding sitei185 – 1851SubstrateBy similarity
Binding sitei398 – 3981SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.7. 3474.
ReactomeiR-MMU-70614. Amino acid synthesis and interconversion (transamination).
R-MMU-71182. Phenylalanine and tyrosine catabolism.
R-MMU-71240. Tryptophan catabolism.
UniPathwayiUPA00334; UER00726.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynurenine--oxoglutarate transaminase 1 (EC:2.6.1.7)
Alternative name(s):
Cysteine-S-conjugate beta-lyase (EC:4.4.1.13)
Glutamine transaminase K
Short name:
GTK
Glutamine--phenylpyruvate transaminase (EC:2.6.1.64)
Kynurenine aminotransferase I
Short name:
KATI
Kynurenine--oxoglutarate transaminase I
Gene namesi
Name:Ccbl1
Synonyms:Kat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1917516. Ccbl1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Kynurenine--oxoglutarate transaminase 1PRO_0000123943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821N6-succinyllysineCombined sources
Modified residuei247 – 2471N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei413 – 4131N6-succinyllysineCombined sources

Proteomic databases

EPDiQ8BTY1.
MaxQBiQ8BTY1.
PaxDbiQ8BTY1.
PRIDEiQ8BTY1.

PTM databases

iPTMnetiQ8BTY1.
PhosphoSiteiQ8BTY1.

Expressioni

Gene expression databases

BgeeiQ8BTY1.
CleanExiMM_CCBL1.
ExpressionAtlasiQ8BTY1. baseline and differential.
GenevisibleiQ8BTY1. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8BTY1. 2 interactions.
MINTiMINT-1868644.
STRINGi10090.ENSMUSP00000038612.

Structurei

3D structure databases

ProteinModelPortaliQ8BTY1.
SMRiQ8BTY1. Positions 4-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0257. Eukaryota.
COG0436. LUCA.
GeneTreeiENSGT00650000093238.
HOGENOMiHOG000223045.
HOVERGENiHBG008391.
InParanoidiQ8BTY1.
KOiK00816.
OMAiFHCPTQA.
OrthoDBiEOG76DTSB.
PhylomeDBiQ8BTY1.
TreeFamiTF105482.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BTY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQLQARRL EGIDHNPWVE FTRLSKEYDV VNLGQGFPDF SPPDFAVQAF
60 70 80 90 100
QQATTGNFML NQYTSAFGYP PLTKILASFF GKLLGQEMDP LKNVLVTVGA
110 120 130 140 150
YGALFTAFQA LVDEGDEVII IEPAFNCYEP MTMMAGGRPV FVSLRLSPAP
160 170 180 190 200
KGQLGSSNDW QLDPTELASK FTPRTKILVL NTPNNPLGKV FSKKELELVA
210 220 230 240 250
ALCQQHDVLC FSDEVYQWLV YDGHQHISIA SLPGMWERTL TIGSAGKSFS
260 270 280 290 300
ATGWKVGWVM GPDNIMKHLR TVHQNSIFHC PTQAQAAVAQ CFEREQQHFG
310 320 330 340 350
QPSSYFLQLP QAMGLNRDHM IQSLQSVGLK PLIPQGSYFL IADISDFKSS
360 370 380 390 400
MPDLPGAMDE PYDTRFAKWM IKNKGLSAIP VSTFYSQPHH KDFDHYIRFC
410 420
FVKDKATLQA MDKRLCSWKG EPQA
Length:424
Mass (Da):47,564
Last modified:March 1, 2003 - v1
Checksum:i5C1B3FE94534805B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901H → R in BAC31248 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042391 mRNA. Translation: BAC31248.1.
AK088404 mRNA. Translation: BAC40333.1.
BC016206 mRNA. Translation: AAH16206.1.
BC052047 mRNA. Translation: AAH52047.1.
CCDSiCCDS15874.1.
RefSeqiNP_765992.2. NM_172404.2.
XP_006498377.2. XM_006498314.2.
UniGeneiMm.216089.

Genome annotation databases

EnsembliENSMUST00000044038; ENSMUSP00000038612; ENSMUSG00000039648.
ENSMUST00000113661; ENSMUSP00000109291; ENSMUSG00000039648.
ENSMUST00000113662; ENSMUSP00000109292; ENSMUSG00000039648.
ENSMUST00000113663; ENSMUSP00000109293; ENSMUSG00000039648.
GeneIDi70266.
KEGGimmu:70266.
UCSCiuc008jbo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042391 mRNA. Translation: BAC31248.1.
AK088404 mRNA. Translation: BAC40333.1.
BC016206 mRNA. Translation: AAH16206.1.
BC052047 mRNA. Translation: AAH52047.1.
CCDSiCCDS15874.1.
RefSeqiNP_765992.2. NM_172404.2.
XP_006498377.2. XM_006498314.2.
UniGeneiMm.216089.

3D structure databases

ProteinModelPortaliQ8BTY1.
SMRiQ8BTY1. Positions 4-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BTY1. 2 interactions.
MINTiMINT-1868644.
STRINGi10090.ENSMUSP00000038612.

PTM databases

iPTMnetiQ8BTY1.
PhosphoSiteiQ8BTY1.

Proteomic databases

EPDiQ8BTY1.
MaxQBiQ8BTY1.
PaxDbiQ8BTY1.
PRIDEiQ8BTY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044038; ENSMUSP00000038612; ENSMUSG00000039648.
ENSMUST00000113661; ENSMUSP00000109291; ENSMUSG00000039648.
ENSMUST00000113662; ENSMUSP00000109292; ENSMUSG00000039648.
ENSMUST00000113663; ENSMUSP00000109293; ENSMUSG00000039648.
GeneIDi70266.
KEGGimmu:70266.
UCSCiuc008jbo.1. mouse.

Organism-specific databases

CTDi883.
MGIiMGI:1917516. Ccbl1.

Phylogenomic databases

eggNOGiKOG0257. Eukaryota.
COG0436. LUCA.
GeneTreeiENSGT00650000093238.
HOGENOMiHOG000223045.
HOVERGENiHBG008391.
InParanoidiQ8BTY1.
KOiK00816.
OMAiFHCPTQA.
OrthoDBiEOG76DTSB.
PhylomeDBiQ8BTY1.
TreeFamiTF105482.

Enzyme and pathway databases

UniPathwayiUPA00334; UER00726.
BRENDAi2.6.1.7. 3474.
ReactomeiR-MMU-70614. Amino acid synthesis and interconversion (transamination).
R-MMU-71182. Phenylalanine and tyrosine catabolism.
R-MMU-71240. Tryptophan catabolism.

Miscellaneous databases

PROiQ8BTY1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BTY1.
CleanExiMM_CCBL1.
ExpressionAtlasiQ8BTY1. baseline and differential.
GenevisibleiQ8BTY1. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
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 and NOD.
    Tissue: Thymus.
  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: C57BL/6J and FVB/N.
    Tissue: Brain and Salivary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Testis.
  4. "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-82 AND LYS-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKAT1_MOUSE
AccessioniPrimary (citable) accession number: Q8BTY1
Secondary accession number(s): Q8BY27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 113 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.