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Q16773

- KAT1_HUMAN

UniProt

Q16773 - KAT1_HUMAN

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Protein

Kynurenine--oxoglutarate transaminase 1

Gene

CCBL1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.1 Publication
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine.1 Publication
An L-cysteine-S-conjugate + H2O = RSH + NH3 + pyruvate.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

Inhibited by tryptophan, indole-3-pyruvic acid, 3-indolepropionic acid, DL-indole-3-lactic acid, indole-3-acetic acid (IAC) and Tris.1 Publication

Pathwayi

Sites

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

GO - Molecular functioni

  1. cysteine-S-conjugate beta-lyase activity Source: UniProtKB-EC
  2. glutamine-phenylpyruvate transaminase activity Source: UniProtKB-EC
  3. kynurenine-oxoglutarate transaminase activity Source: UniProtKB
  4. L-glutamine:pyruvate aminotransferase activity Source: Reactome
  5. L-phenylalanine:pyruvate aminotransferase activity Source: Reactome
  6. L-phenylalanine-oxaloacetate transaminase activity Source: Reactome
  7. protein homodimerization activity Source: UniProtKB
  8. pyridoxal phosphate binding Source: InterPro
  9. transaminase activity Source: ProtInc

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: Reactome
  2. cellular modified amino acid metabolic process Source: ProtInc
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. kynurenine metabolic process Source: UniProtKB
  5. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  6. L-phenylalanine catabolic process Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. tryptophan catabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS10240-MONOMER.
BRENDAi2.6.1.7. 2681.
ReactomeiREACT_121117. Abnormal metabolism in phenylketonuria.
REACT_1786. Phenylalanine and tyrosine catabolism.
REACT_238. Amino acid synthesis and interconversion (transamination).
REACT_916. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:1564. CCBL1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Kynurenine--oxoglutarate transaminase 1PRO_0000123942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei247 – 2471N6-(pyridoxal phosphate)lysine

Proteomic databases

MaxQBiQ16773.
PaxDbiQ16773.
PRIDEiQ16773.

PTM databases

PhosphoSiteiQ16773.

Expressioni

Gene expression databases

BgeeiQ16773.
CleanExiHS_CCBL1.
ExpressionAtlasiQ16773. baseline and differential.
GenevestigatoriQ16773.

Organism-specific databases

HPAiHPA021176.
HPA021177.
HPA027736.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi107326. 2 interactions.
STRINGi9606.ENSP00000302227.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi17 – 2610Combined sources
Helixi44 – 5512Combined sources
Helixi58 – 614Combined sources
Helixi70 – 8415Combined sources
Helixi90 – 934Combined sources
Beta strandi94 – 985Combined sources
Helixi99 – 11113Combined sources
Beta strandi117 – 1237Combined sources
Helixi128 – 1347Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi154 – 1563Combined sources
Helixi157 – 1593Combined sources
Helixi164 – 1685Combined sources
Beta strandi175 – 1839Combined sources
Turni185 – 1873Combined sources
Helixi193 – 20614Combined sources
Beta strandi209 – 2135Combined sources
Turni215 – 2184Combined sources
Helixi229 – 2313Combined sources
Turni233 – 2353Combined sources
Helixi236 – 2383Combined sources
Beta strandi239 – 2446Combined sources
Helixi245 – 2495Combined sources
Helixi252 – 2543Combined sources
Beta strandi257 – 2604Combined sources
Helixi263 – 27412Combined sources
Turni275 – 2773Combined sources
Helixi282 – 29716Combined sources
Turni298 – 3003Combined sources
Helixi305 – 32521Combined sources
Turni326 – 3283Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi335 – 3439Combined sources
Helixi345 – 3506Combined sources
Helixi362 – 37413Combined sources
Helixi381 – 3844Combined sources
Helixi387 – 3904Combined sources
Turni391 – 3933Combined sources
Beta strandi395 – 4006Combined sources
Helixi405 – 42016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ16773.
SMRiQ16773. Positions 4-422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16773.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093238.
HOVERGENiHBG008391.
InParanoidiQ16773.
KOiK00816.
OrthoDBiEOG76DTSB.
PhylomeDBiQ16773.
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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16773-1) [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
MAKQLQARRL DGIDYNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF
60 70 80 90 100
QHAVSGDFML NQYTKTFGYP PLTKILASFF GELLGQEIDP LRNVLVTVGG
110 120 130 140 150
YGALFTAFQA LVDEGDEVII IEPFFDCYEP MTMMAGGRPV FVSLKPGPIQ
160 170 180 190 200
NGELGSSSNW QLDPMELAGK FTSRTKALVL NTPNNPLGKV FSREELELVA
210 220 230 240 250
SLCQQHDVVC ITDEVYQWMV YDGHQHISIA SLPGMWERTL TIGSAGKTFS
260 270 280 290 300
ATGWKVGWVL GPDHIMKHLR TVHQNSVFHC PTQSQAAVAE SFEREQLLFR
310 320 330 340 350
QPSSYFVQFP QAMQRCRDHM IRSLQSVGLK PIIPQGSYFL ITDISDFKRK
360 370 380 390 400
MPDLPGAVDE PYDRRFVKWM IKNKGLVAIP VSIFYSVPHQ KHFDHYIRFC
410 420
FVKDEATLQA MDEKLRKWKV EL
Length:422
Mass (Da):47,875
Last modified:November 1, 1996 - v1
Checksum:iEAEF2F5E77A9B55A
GO
Isoform 2 (identifier: Q16773-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-117: Missing.

Show »
Length:372
Mass (Da):42,550
Checksum:iAAD732B1797B180C
GO
Isoform 3 (identifier: Q16773-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:250
Mass (Da):27,420
Checksum:iB431352A3ECB8B8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti422 – 4221L → LWP in AAH33685. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 11750Missing in isoform 2. 1 PublicationVSP_009875Add
BLAST
Alternative sequencei230 – 25021ASLPG…GKTFS → VSAAVLFGLGQPASLACGNG P in isoform 3. 1 PublicationVSP_009876Add
BLAST
Alternative sequencei251 – 422172Missing in isoform 3. 1 PublicationVSP_009877Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43884.1. [Q16773-1]
CCDS48038.1. [Q16773-2]
PIRiS69001. S52790.
RefSeqiNP_001116143.1. NM_001122671.1. [Q16773-1]
NP_001116144.1. NM_001122672.1. [Q16773-2]
NP_004050.3. NM_004059.4. [Q16773-1]
UniGeneiHs.495250.

Genome annotation databases

EnsembliENST00000302586; ENSP00000302227; ENSG00000171097. [Q16773-1]
ENST00000320665; ENSP00000317342; ENSG00000171097. [Q16773-2]
GeneIDi883.
KEGGihsa:883.
UCSCiuc004bwh.3. human. [Q16773-1]
uc004bwj.3. human. [Q16773-2]

Polymorphism databases

DMDMi46396284.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS43884.1. [Q16773-1 ]
CCDS48038.1. [Q16773-2 ]
PIRi S69001. S52790.
RefSeqi NP_001116143.1. NM_001122671.1. [Q16773-1 ]
NP_001116144.1. NM_001122672.1. [Q16773-2 ]
NP_004050.3. NM_004059.4. [Q16773-1 ]
UniGenei Hs.495250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W7L X-ray 2.00 A 1-422 [» ]
1W7M X-ray 2.70 A 1-422 [» ]
1W7N X-ray 2.90 A 1-422 [» ]
3FVS X-ray 1.50 A/B 1-422 [» ]
3FVU X-ray 1.55 A/B 1-422 [» ]
3FVX X-ray 1.50 A/B 1-422 [» ]
ProteinModelPortali Q16773.
SMRi Q16773. Positions 4-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107326. 2 interactions.
STRINGi 9606.ENSP00000302227.

Chemistry

BindingDBi Q16773.
ChEMBLi CHEMBL3962.
DrugBanki DB00130. L-Glutamine.

PTM databases

PhosphoSitei Q16773.

Polymorphism databases

DMDMi 46396284.

Proteomic databases

MaxQBi Q16773.
PaxDbi Q16773.
PRIDEi Q16773.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302586 ; ENSP00000302227 ; ENSG00000171097 . [Q16773-1 ]
ENST00000320665 ; ENSP00000317342 ; ENSG00000171097 . [Q16773-2 ]
GeneIDi 883.
KEGGi hsa:883.
UCSCi uc004bwh.3. human. [Q16773-1 ]
uc004bwj.3. human. [Q16773-2 ]

Organism-specific databases

CTDi 883.
GeneCardsi GC09M131595.
H-InvDB HIX0008439.
HGNCi HGNC:1564. CCBL1.
HPAi HPA021176.
HPA021177.
HPA027736.
MIMi 600547. gene.
neXtProti NX_Q16773.
PharmGKBi PA26138.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0436.
GeneTreei ENSGT00650000093238.
HOVERGENi HBG008391.
InParanoidi Q16773.
KOi K00816.
OrthoDBi EOG76DTSB.
PhylomeDBi Q16773.
TreeFami TF105482.

Enzyme and pathway databases

UniPathwayi UPA00334 ; UER00726 .
BioCyci MetaCyc:HS10240-MONOMER.
BRENDAi 2.6.1.7. 2681.
Reactomei REACT_121117. Abnormal metabolism in phenylketonuria.
REACT_1786. Phenylalanine and tyrosine catabolism.
REACT_238. Amino acid synthesis and interconversion (transamination).
REACT_916. Tryptophan catabolism.

Miscellaneous databases

ChiTaRSi CCBL1. human.
EvolutionaryTracei Q16773.
GeneWikii CCBL1.
GenomeRNAii 883.
NextBioi 3654.
PROi Q16773.
SOURCEi Search...

Gene expression databases

Bgeei Q16773.
CleanExi HS_CCBL1.
ExpressionAtlasi Q16773. baseline and differential.
Genevestigatori Q16773.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiKAT1_HUMAN
AccessioniPrimary (citable) accession number: Q16773
Secondary accession number(s): Q5T275, Q8N191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3