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Q16773 (KAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
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 names
Name:CCBL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. Ref.5

L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. Ref.5

RS-CH(2)-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate. Ref.5

Cofactor

Pyridoxal phosphate. Ref.4 Ref.5

Enzyme regulation

Inhibited by tryptophan, indole-3-pyruvic acid, 3-indolepropionic acid, DL-indole-3-lactic acid, indole-3-acetic acid (IAC) and Tris. Ref.5

Pathway

Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Lyase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

L-phenylalanine catabolic process

Traceable author statement. Source: Reactome

cellular amino acid biosynthetic process

Traceable author statement. Source: Reactome

cellular modified amino acid metabolic process

Traceable author statement Ref.1. Source: ProtInc

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

kynurenine metabolic process

Inferred from direct assay Ref.5. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

tryptophan catabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionL-glutamine:pyruvate aminotransferase activity

Inferred from experiment. Source: Reactome

L-phenylalanine-oxaloacetate transaminase activity

Traceable author statement. Source: Reactome

L-phenylalanine:pyruvate aminotransferase activity

Inferred from experiment. Source: Reactome

cysteine-S-conjugate beta-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamine-phenylpyruvate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

kynurenine-oxoglutarate transaminase activity

Inferred from direct assay Ref.5. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.4. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16773-1)

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: Q16773-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-117: Missing.
Isoform 3 (identifier: Q16773-3)

The sequence of this isoform differs from the canonical sequence as follows:
     230-250: ASLPGMWERTLTIGSAGKTFS → VSAAVLFGLGQPASLACGNGP
     251-422: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Kynurenine--oxoglutarate transaminase 1
PRO_0000123942

Sites

Binding site361Substrate; via amide nitrogen
Binding site1851Substrate
Binding site3981Substrate

Amino acid modifications

Modified residue2471N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence68 – 11750Missing in isoform 2.
VSP_009875
Alternative sequence230 – 25021ASLPG…GKTFS → VSAAVLFGLGQPASLACGNG P in isoform 3.
VSP_009876
Alternative sequence251 – 422172Missing in isoform 3.
VSP_009877

Experimental info

Sequence conflict4221L → LWP in AAH33685. Ref.3

Secondary structure

.......................................................................... 422
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: EAEF2F5E77A9B55A

FASTA42247,875
        10         20         30         40         50         60 
MAKQLQARRL DGIDYNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF QHAVSGDFML 

        70         80         90        100        110        120 
NQYTKTFGYP PLTKILASFF GELLGQEIDP LRNVLVTVGG YGALFTAFQA LVDEGDEVII 

       130        140        150        160        170        180 
IEPFFDCYEP MTMMAGGRPV FVSLKPGPIQ NGELGSSSNW QLDPMELAGK FTSRTKALVL 

       190        200        210        220        230        240 
NTPNNPLGKV FSREELELVA SLCQQHDVVC ITDEVYQWMV YDGHQHISIA SLPGMWERTL 

       250        260        270        280        290        300 
TIGSAGKTFS ATGWKVGWVL GPDHIMKHLR TVHQNSVFHC PTQSQAAVAE SFEREQLLFR 

       310        320        330        340        350        360 
QPSSYFVQFP QAMQRCRDHM IRSLQSVGLK PIIPQGSYFL ITDISDFKRK MPDLPGAVDE 

       370        380        390        400        410        420 
PYDRRFVKWM IKNKGLVAIP VSIFYSVPHQ KHFDHYIRFC FVKDEATLQA MDEKLRKWKV 


EL 

« Hide

Isoform 2 [UniParc].

Checksum: AAD732B1797B180C
Show »

FASTA37242,550
Isoform 3 [UniParc].

Checksum: B431352A3ECB8B8B
Show »

FASTA25027,420

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase."
Perry S., Harries H., Scholfield C., Lock E., King L., Gibson G., Goldfarb P.
FEBS Lett. 360:277-280(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2 AND 3).
Tissue: Brain and Muscle.
[4]"Crystal structure of human kynurenine aminotransferase I."
Rossi F., Han Q., Li J., Li J., Rizzi M.
J. Biol. Chem. 279:50214-50220(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND PHENYLALANINE, SUBUNIT, COFACTOR.
[5]"Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K."
Han Q., Robinson H., Cai T., Tagle D.A., Li J.
J. Med. Chem. 52:2786-2793(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND THE INHIBITORS INDOLEACETIC ACID AND TRIS, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82224 mRNA. Translation: CAA57702.1.
AL441992 Genomic DNA. Translation: CAI15414.1.
AL441992 Genomic DNA. Translation: CAI15415.1.
BC021262 mRNA. Translation: AAH21262.1.
BC033685 mRNA. Translation: AAH33685.1.
CCDSCCDS43884.1. [Q16773-1]
CCDS48038.1. [Q16773-2]
PIRS52790. S69001.
RefSeqNP_001116143.1. NM_001122671.1. [Q16773-1]
NP_001116144.1. NM_001122672.1. [Q16773-2]
NP_004050.3. NM_004059.4. [Q16773-1]
UniGeneHs.495250.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W7LX-ray2.00A1-422[»]
1W7MX-ray2.70A1-422[»]
1W7NX-ray2.90A1-422[»]
3FVSX-ray1.50A/B1-422[»]
3FVUX-ray1.55A/B1-422[»]
3FVXX-ray1.50A/B1-422[»]
ProteinModelPortalQ16773.
SMRQ16773. Positions 4-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107326. 2 interactions.
STRING9606.ENSP00000302227.

Chemistry

BindingDBQ16773.
ChEMBLCHEMBL3962.
DrugBankDB00130. L-Glutamine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteQ16773.

Polymorphism databases

DMDM46396284.

Proteomic databases

MaxQBQ16773.
PaxDbQ16773.
PRIDEQ16773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302586; ENSP00000302227; ENSG00000171097. [Q16773-1]
ENST00000320665; ENSP00000317342; ENSG00000171097. [Q16773-2]
GeneID883.
KEGGhsa:883.
UCSCuc004bwh.3. human. [Q16773-1]
uc004bwj.3. human. [Q16773-2]

Organism-specific databases

CTD883.
GeneCardsGC09M131595.
H-InvDBHIX0008439.
HGNCHGNC:1564. CCBL1.
HPAHPA021176.
HPA021177.
HPA027736.
MIM600547. gene.
neXtProtNX_Q16773.
PharmGKBPA26138.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0436.
HOVERGENHBG008391.
InParanoidQ16773.
KOK00816.
OrthoDBEOG76DTSB.
PhylomeDBQ16773.
TreeFamTF105482.

Enzyme and pathway databases

BioCycMetaCyc:HS10240-MONOMER.
BRENDA2.6.1.7. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00334; UER00726.

Gene expression databases

ArrayExpressQ16773.
BgeeQ16773.
CleanExHS_CCBL1.
GenevestigatorQ16773.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ16773.
GeneWikiCCBL1.
GenomeRNAi883.
NextBio3654.
PROQ16773.
SOURCESearch...

Entry information

Entry nameKAT1_HUMAN
AccessionPrimary (citable) accession number: Q16773
Secondary accession number(s): Q5T275, Q8N191
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 125 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM