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Protein

Kynurenine--oxoglutarate transaminase 1

Gene

KYAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: 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 (KYAT1)
  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)DescriptionActionsGraphical viewLength
Binding sitei36Substrate; via amide nitrogen1
Binding sitei185Substrate1
Binding sitei398Substrate1

GO - Molecular functioni

  • cysteine-S-conjugate beta-lyase activity Source: FlyBase
  • glutamine-phenylpyruvate transaminase activity Source: UniProtKB-EC
  • kynurenine-oxoglutarate transaminase activity Source: UniProtKB
  • L-glutamine:pyruvate aminotransferase activity Source: Reactome
  • L-phenylalanine:pyruvate aminotransferase activity Source: Reactome
  • protein homodimerization activity Source: UniProtKB
  • pyridoxal phosphate binding Source: InterPro
  • transaminase activity Source: ProtInc

GO - Biological processi

Keywordsi

Molecular functionAminotransferase, Lyase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS10240-MONOMER
BRENDAi2.6.1.7 2681
ReactomeiR-HSA-70614 Amino acid synthesis and interconversion (transamination)
R-HSA-71182 Phenylalanine and tyrosine catabolism
R-HSA-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 1Imported
Kynurenine aminotransferase I
Short name:
KATI
Kynurenine--oxoglutarate transaminase I
Gene namesi
Name:KYAT1Imported
Synonyms:CCBL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000171097.13
HGNCiHGNC:1564 KYAT1
MIMi600547 gene
neXtProtiNX_Q16773

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi883
OpenTargetsiENSG00000171097
PharmGKBiPA26138

Chemistry databases

ChEMBLiCHEMBL3962
DrugBankiDB07950 1H-INDOL-3-YLACETIC ACID
DB02556 D-Phenylalanine
DB00130 L-Glutamine
DB04083 N'-Pyridoxyl-Lysine-5'-Monophosphate
DB00114 Pyridoxal Phosphate
DB02142 Pyridoxamine-5'-Phosphate
GuidetoPHARMACOLOGYi1445

Polymorphism and mutation databases

BioMutaiCCBL1
DMDMi46396284

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239421 – 422Kynurenine--oxoglutarate transaminase 1Add BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei247N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiQ16773
MaxQBiQ16773
PaxDbiQ16773
PeptideAtlasiQ16773
PRIDEiQ16773

PTM databases

iPTMnetiQ16773
PhosphoSitePlusiQ16773

Expressioni

Gene expression databases

BgeeiENSG00000171097
CleanExiHS_CCBL1
ExpressionAtlasiQ16773 baseline and differential
GenevisibleiQ16773 HS

Organism-specific databases

HPAiHPA021176
HPA021177
HPA027736

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi107326, 11 interactors
IntActiQ16773, 2 interactors
STRINGi9606.ENSP00000302227

Chemistry databases

BindingDBiQ16773

Structurei

Secondary structure

1422
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Helixi18 – 26Combined sources9
Helixi44 – 55Combined sources12
Helixi58 – 61Combined sources4
Helixi70 – 84Combined sources15
Turni90 – 92Combined sources3
Beta strandi93 – 98Combined sources6
Helixi99 – 111Combined sources13
Beta strandi117 – 123Combined sources7
Helixi128 – 134Combined sources7
Beta strandi138 – 143Combined sources6
Beta strandi151 – 153Combined sources3
Beta strandi154 – 156Combined sources3
Helixi157 – 159Combined sources3
Helixi164 – 170Combined sources7
Beta strandi175 – 183Combined sources9
Turni185 – 187Combined sources3
Helixi193 – 206Combined sources14
Beta strandi209 – 213Combined sources5
Turni215 – 218Combined sources4
Helixi229 – 231Combined sources3
Turni233 – 235Combined sources3
Helixi236 – 238Combined sources3
Beta strandi239 – 244Combined sources6
Helixi245 – 248Combined sources4
Helixi252 – 254Combined sources3
Beta strandi257 – 260Combined sources4
Helixi263 – 274Combined sources12
Turni275 – 277Combined sources3
Helixi282 – 297Combined sources16
Turni298 – 300Combined sources3
Helixi305 – 325Combined sources21
Turni326 – 328Combined sources3
Beta strandi330 – 333Combined sources4
Beta strandi335 – 343Combined sources9
Helixi345 – 350Combined sources6
Helixi362 – 374Combined sources13
Helixi381 – 384Combined sources4
Helixi387 – 390Combined sources4
Turni391 – 393Combined sources3
Beta strandi395 – 400Combined sources6
Helixi405 – 420Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WLHX-ray1.28A/B1-422[»]
4WLJX-ray1.54A/B1-422[»]
4WP0X-ray3.00A/B/C/D1-422[»]
ProteinModelPortaliQ16773
SMRiQ16773
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16773

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0257 Eukaryota
COG0436 LUCA
GeneTreeiENSGT00650000093238
HOVERGENiHBG008391
InParanoidiQ16773
KOiK00816
PhylomeDBiQ16773
TreeFamiTF105482

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
InterProiView protein in InterPro
IPR004839 Aminotransferase_I/II
IPR034614 KAT_I
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR43807:SF14 PTHR43807:SF14, 1 hit
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti422L → LWP in AAH33685 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00987568 – 117Missing in isoform 2. 1 PublicationAdd BLAST50
Alternative sequenceiVSP_009876230 – 250ASLPG…GKTFS → VSAAVLFGLGQPASLACGNG P in isoform 3. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_009877251 – 422Missing in isoform 3. 1 PublicationAdd BLAST172

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82224 mRNA Translation: CAA57702.1
AL441992 Genomic DNA No translation available.
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]
XP_011517470.1, XM_011519168.1 [Q16773-1]
XP_011517471.1, XM_011519169.1 [Q16773-1]
XP_011517472.1, XM_011519170.2 [Q16773-1]
XP_016870754.1, XM_017015265.1 [Q16773-1]
XP_016870755.1, XM_017015266.1
XP_016870756.1, XM_017015267.1 [Q16773-1]
XP_016870757.1, XM_017015268.1
UniGeneiHs.495250

Genome annotation databases

EnsembliENST00000302586; ENSP00000302227; ENSG00000171097 [Q16773-1]
ENST00000320665; ENSP00000317342; ENSG00000171097 [Q16773-2]
GeneIDi883
KEGGihsa:883
UCSCiuc004bwh.5 human [Q16773-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiKAT1_HUMAN
AccessioniPrimary (citable) accession number: Q16773
Secondary accession number(s): Q5T275, Q8N191
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 156 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health