Q16773 (KAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CCBL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Lyase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-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 tryptophan catabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular_function	L-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: EC glutamine-phenylpyruvate transaminase activity Inferred from electronic annotation. Source: EC kynurenine-oxoglutarate transaminase activity Inferred from direct assay Ref.5. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 422

422

Kynurenine--oxoglutarate transaminase 1

PRO_0000123942

Sites

Binding site

36

1

Substrate; via amide nitrogen

Binding site

185

1

Substrate

Binding site

398

1

Substrate

Amino acid modifications

Modified residue

247

1

N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence

68 – 117

50

Missing in isoform 2.

VSP_009875

Alternative sequence

230 – 250

21

ASLPG…GKTFS → VSAAVLFGLGQPASLACGNG P in isoform 3.

VSP_009876

Alternative sequence

251 – 422

172

Missing in isoform 3.

VSP_009877

Experimental info

Sequence conflict

422

1

L → LWP in AAH33685. Ref.3

Secondary structure

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422

Helix Strand Turn

Details...

Helix

8 – 10

3

Helix

17 – 26

10

Helix

44 – 55

12

Helix

58 – 61

4

Helix

70 – 84

15

Helix

90 – 93

4

Beta strand

94 – 98

5

Helix

99 – 111

13

Beta strand

117 – 123

7

Helix

128 – 134

7

Beta strand

138 – 143

6

Beta strand

151 – 153

3

Beta strand

154 – 156

3

Helix

157 – 159

3

Helix

164 – 168

5

Beta strand

175 – 183

9

Turn

185 – 187

3

Helix

193 – 206

14

Beta strand

209 – 213

5

Turn

215 – 218

4

Helix

229 – 231

3

Turn

233 – 235

3

Helix

236 – 238

3

Beta strand

239 – 244

6

Helix

245 – 249

5

Helix

252 – 254

3

Beta strand

257 – 260

4

Helix

263 – 274

12

Turn

275 – 277

3

Helix

282 – 297

16

Turn

298 – 300

3

Helix

305 – 325

21

Turn

326 – 328

3

Beta strand

330 – 333

4

Beta strand

335 – 343

9

Helix

345 – 350

6

Helix

362 – 374

13

Helix

381 – 384

4

Helix

387 – 390

4

Turn

391 – 393

3

Beta strand

395 – 400

6

Helix

405 – 420

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EAEF2F5E77A9B55A	FASTA	422	47,875
	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
	Isoform 2 [UniParc]. Checksum: AAD732B1797B180C	FASTA	372	42,550
	10 20 30 40 50 60 MAKQLQARRL DGIDYNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF QHAVSGDFML 70 80 90 100 110 120 NQYTKTFVII IEPFFDCYEP MTMMAGGRPV FVSLKPGPIQ NGELGSSSNW QLDPMELAGK 130 140 150 160 170 180 FTSRTKALVL NTPNNPLGKV FSREELELVA SLCQQHDVVC ITDEVYQWMV YDGHQHISIA 190 200 210 220 230 240 SLPGMWERTL TIGSAGKTFS ATGWKVGWVL GPDHIMKHLR TVHQNSVFHC PTQSQAAVAE 250 260 270 280 290 300 SFEREQLLFR QPSSYFVQFP QAMQRCRDHM IRSLQSVGLK PIIPQGSYFL ITDISDFKRK 310 320 330 340 350 360 MPDLPGAVDE PYDRRFVKWM IKNKGLVAIP VSIFYSVPHQ KHFDHYIRFC FVKDEATLQA 370 MDEKLRKWKV EL
	Isoform 3 [UniParc]. Checksum: B431352A3ECB8B8B	FASTA	250	27,420
	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 YDGHQHISIV SAAVLFGLGQ 250 PASLACGNGP

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00181795.
IPI00410254.
IPI01014100.

PIR

S52790. S69001.

RefSeq

NP_001116143.1. NM_001122671.1.
NP_001116144.1. NM_001122672.1.
NP_004050.3. NM_004059.4.

UniGene

Hs.495250.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16773.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000302227.

PTM databases

PhosphoSite

Q16773.

Polymorphism databases

DMDM

46396284.

Proteomic databases

PaxDb

Q16773.

PRIDE

Q16773.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302586; ENSP00000302227; ENSG00000171097.
ENST00000320665; ENSP00000317342; ENSG00000171097.

GeneID

883.

KEGG

hsa:883.

UCSC

uc004bwh.3. human.
uc004bwj.3. human.

Organism-specific databases

CTD

883.

GeneCards

GC09M131595.

H-InvDB

HIX0008439.

HGNC

HGNC:1564. CCBL1.

HPA

HPA021176.
HPA021177.
HPA027736.

MIM

600547. gene.

neXtProt

NX_Q16773.

PharmGKB

PA26138.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0436.

HOVERGEN

HBG008391.

InParanoid

Q16773.

KO

K00816.

OrthoDB

EOG44QT0Z.

PhylomeDB

Q16773.

Enzyme and pathway databases

BioCyc

MetaCyc:HS10240-MONOMER.

BRENDA

2.6.1.7. 2681.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

UniPathway

UPA00334; UER00726.

Gene expression databases

ArrayExpress

Q16773.

Bgee

Q16773.

CleanEx

HS_CCBL1.

Genevestigator

Q16773.

GermOnline

ENSG00000171097. Homo sapiens.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q16773.

ChEMBL

CHEMBL3962.

DrugBank

DB00130. L-Glutamine.
DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

Q16773.

GenomeRNAi

883.

NextBio

3654.

SOURCE

Search...

Entry information

Entry name

KAT1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.