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Q16773

- KAT1_HUMAN

UniProt

Q16773 - KAT1_HUMAN

Protein

Kynurenine--oxoglutarate transaminase 1

Gene

CCBL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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
    RS-CH(2)-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate.1 Publication

    Cofactori

    Pyridoxal phosphate.2 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

    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

    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

    ArrayExpressiQ16773.
    BgeeiQ16773.
    CleanExiHS_CCBL1.
    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 – 103
    Helixi17 – 2610
    Helixi44 – 5512
    Helixi58 – 614
    Helixi70 – 8415
    Helixi90 – 934
    Beta strandi94 – 985
    Helixi99 – 11113
    Beta strandi117 – 1237
    Helixi128 – 1347
    Beta strandi138 – 1436
    Beta strandi151 – 1533
    Beta strandi154 – 1563
    Helixi157 – 1593
    Helixi164 – 1685
    Beta strandi175 – 1839
    Turni185 – 1873
    Helixi193 – 20614
    Beta strandi209 – 2135
    Turni215 – 2184
    Helixi229 – 2313
    Turni233 – 2353
    Helixi236 – 2383
    Beta strandi239 – 2446
    Helixi245 – 2495
    Helixi252 – 2543
    Beta strandi257 – 2604
    Helixi263 – 27412
    Turni275 – 2773
    Helixi282 – 29716
    Turni298 – 3003
    Helixi305 – 32521
    Turni326 – 3283
    Beta strandi330 – 3334
    Beta strandi335 – 3439
    Helixi345 – 3506
    Helixi362 – 37413
    Helixi381 – 3844
    Helixi387 – 3904
    Turni391 – 3933
    Beta strandi395 – 4006
    Helixi405 – 42016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MAKQLQARRL DGIDYNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF    50
    QHAVSGDFML NQYTKTFGYP PLTKILASFF GELLGQEIDP LRNVLVTVGG 100
    YGALFTAFQA LVDEGDEVII IEPFFDCYEP MTMMAGGRPV FVSLKPGPIQ 150
    NGELGSSSNW QLDPMELAGK FTSRTKALVL NTPNNPLGKV FSREELELVA 200
    SLCQQHDVVC ITDEVYQWMV YDGHQHISIA SLPGMWERTL TIGSAGKTFS 250
    ATGWKVGWVL GPDHIMKHLR TVHQNSVFHC PTQSQAAVAE SFEREQLLFR 300
    QPSSYFVQFP QAMQRCRDHM IRSLQSVGLK PIIPQGSYFL ITDISDFKRK 350
    MPDLPGAVDE PYDRRFVKWM IKNKGLVAIP VSIFYSVPHQ KHFDHYIRFC 400
    FVKDEATLQA MDEKLRKWKV EL 422
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

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

    Gene expression databases

    ArrayExpressi Q16773.
    Bgeei Q16773.
    CleanExi HS_CCBL1.
    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

    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: October 1, 2014
    This is version 127 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