Reviewed, UniProtKB/Swiss-Prot Q16773 (KAT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Kynurenine--oxoglutarate transaminase 1
    EC=2.6.1.7
Alternative name(s):
    Kynurenine--oxoglutarate transaminase I
    Kynurenine aminotransferase I
      Short name=KATI
    Glutamine--phenylpyruvate transaminase
    EC=2.6.1.64
    Glutamine transaminase K
      Short name=GTK
    Cysteine-S-conjugate beta-lyase
    EC=4.4.1.13

Gene names

Name:

CCBL1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 By similarity.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. RS-CH(2)-CH(NH3+)COO- = RSH + NH3 + pyruvate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
Subunit structure	Homodimer By similarity.
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
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid derivative metabolic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Ref.1 Traceable author statement. Source: ProtInc
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro 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 electronic annotation. Source: EC 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

Amino acid modifications

Modified residue

247

1

N6-(pyridoxal phosphate)lysine By similarity

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

18 – 26

9

Helix

44 – 53

10

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

154 – 156

3

Helix

157 – 159

3

Helix

164 – 170

7

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 – 248

4

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

Beta strand

395 – 400

6

Helix

405 – 419

15

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. 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. 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: 7883047] [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: 15164053] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Brain and Muscle.
+	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

IPI00002523.
IPI00181795.
IPI00410254.

PIR

S52790. S69001.

RefSeq

NP_001116143.1.
NP_001116144.1.
NP_004050.3.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q16773.

Proteomic databases

PRIDE

Q16773.

Genome annotation databases

Ensembl

ENST00000302586; ENSP00000302227; ENSG00000171097; Homo sapiens. [Genome view]
ENST00000436267; ENSP00000399415; ENSG00000171097; Homo sapiens. [Genome view]

GeneID

883.

KEGG

hsa:883.

UCSC

uc004bwh.1. human.

Organism-specific databases

CTD

883.

GeneCards

GC09M130635.

HGNC

HGNC:1564. CCBL1.

HPA

HPA021176.
HPA021177.

MIM

600547. gene.

PharmGKB

PA26138.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16237.

HOVERGEN

Q16773.

InParanoid

Q16773.

OMA

HICFAVE.

PhylomeDB

Q16773.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15006.

BRENDA

2.6.1.64. 247.
2.6.1.7. 247.
4.4.1.13. 247.

Gene expression databases

ArrayExpress

Q16773.

Bgee

Q16773.

CleanEx

HS_CCBL1.

Genevestigator

Q16773.

GermOnline

ENSG00000171097. Homo sapiens.

Family and domain databases

InterPro

IPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00753. ACCSYNTHASE.

ProtoNet

Search...

Other Resources

DrugBank

DB00130. L-Glutamine.
DB00114. Pyridoxal Phosphate.

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:	January 19, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.