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O75600

- KBL_HUMAN

UniProt

O75600 - KBL_HUMAN

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Protein
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Gene
GCAT, KBL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate.UniRule annotation

Cofactori

Pyridoxal phosphate By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei159 – 1591Substrate By similarity
Binding sitei206 – 2061Pyridoxal phosphate By similarity
Binding sitei389 – 3891Substrate By similarity

GO - Molecular functioni

  1. glycine C-acetyltransferase activity Source: UniProtKB
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. L-threonine catabolic process to glycine Source: UniProtKB-UniPathway
  2. biosynthetic process Source: InterPro
  3. cellular amino acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00046; UER00506.

Names & Taxonomyi

Protein namesi
Recommended name:
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial (EC:2.3.1.29)
Short name:
AKB ligase
Alternative name(s):
Aminoacetone synthase
Glycine acetyltransferase
Gene namesi
Name:GCAT
Synonyms:KBL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4188. GCAT.

Subcellular locationi

Mitochondrion By similarity. Nucleus
Note: Translocates to the nucleus upon cold and osmotic stress.1 Publication

GO - Cellular componenti

  1. mitochondrion Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28603.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121Mitochondrion By similarity
Add
BLAST
Chaini22 – 4193982-amino-3-ketobutyrate coenzyme A ligase, mitochondrialUniRule annotation
PRO_0000001246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-acetyllysine; alternate By similarity
Modified residuei45 – 451N6-succinyllysine; alternate By similarity
Modified residuei187 – 1871N6-acetyllysine; alternate By similarity
Modified residuei187 – 1871N6-succinyllysine; alternate By similarity
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysine Inferred
Modified residuei326 – 3261N6-succinyllysine By similarity
Modified residuei368 – 3681N6-succinyllysine By similarity
Modified residuei383 – 3831N6-acetyllysine; alternate By similarity
Modified residuei383 – 3831N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75600.
PaxDbiO75600.
PRIDEiO75600.

PTM databases

PhosphoSiteiO75600.

Expressioni

Tissue specificityi

Strongly expressed in heart, brain, liver and pancreas. Also found in lung.1 Publication

Gene expression databases

ArrayExpressiO75600.
BgeeiO75600.
CleanExiHS_GCAT.
GenevestigatoriO75600.

Organism-specific databases

HPAiHPA020460.

Interactioni

Protein-protein interaction databases

BioGridi117027. 6 interactions.
IntActiO75600. 2 interactions.
STRINGi9606.ENSP00000248924.

Structurei

3D structure databases

ProteinModelPortaliO75600.
SMRiO75600. Positions 21-418.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1352Pyridoxal phosphate binding By similarity
Regioni262 – 2654Pyridoxal phosphate binding By similarity
Regioni295 – 2962Pyridoxal phosphate binding; shared with dimeric partner By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221022.
HOVERGENiHBG105208.
KOiK00639.
OMAiICDAHGA.
OrthoDBiEOG79GT68.
PhylomeDBiO75600.
TreeFamiTF105923.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00985. 2am3keto_CoA_ligase.
InterProiIPR011282. 2am3keto_CoA_ligase.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. 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.
TIGRFAMsiTIGR01822. 2am3keto_CoA. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75600-1) [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

MWPGNAWRAA LFWVPRGRRA QSALAQLRGI LEGELEGIRG AGTWKSERVI    50
TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS 100
SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED 150
AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA 200
TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL 250
GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP 300
AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP 350
VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED 400
IDRCVEAFVE VGRLHGALP 419
Length:419
Mass (Da):45,285
Last modified:November 1, 1998 - v1
Checksum:iC7760699E0474821
GO
Isoform 2 (identifier: O75600-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-65: G → GGPGTVIFPGLPLPHLSCCIHLLSFTS

Note: No experimental confirmation available.

Show »
Length:445
Mass (Da):47,974
Checksum:i5AD82BF1119ADC87
GO

Sequence cautioni

The sequence BAC85552.1 differs from that shown. Reason: Frameshift at position 232.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391R → C.
Corresponds to variant rs710187 [ dbSNP | Ensembl ].
VAR_015094
Natural varianti100 – 1001S → N.
Corresponds to variant rs34468367 [ dbSNP | Ensembl ].
VAR_048229

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 651G → GGPGTVIFPGLPLPHLSCCI HLLSFTS in isoform 2.
VSP_044607

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3871R → W in AAH14457. 1 Publication
Isoform 2 (identifier: O75600-2)
Sequence conflicti77 – 771L → S in BAC85552. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077740 mRNA. Translation: AAC27720.1.
AK123190 mRNA. Translation: BAC85552.1. Frameshift.
Z97630 Genomic DNA. Translation: CAB42830.1.
Z97630 Genomic DNA. Translation: CAX14890.1.
BC014457 mRNA. Translation: AAH14457.1.
CCDSiCCDS13957.1. [O75600-1]
CCDS54527.1. [O75600-2]
RefSeqiNP_001165161.1. NM_001171690.1. [O75600-2]
NP_055106.1. NM_014291.3. [O75600-1]
XP_005261467.1. XM_005261410.2. [O75600-2]
UniGeneiHs.54609.

Genome annotation databases

EnsembliENST00000248924; ENSP00000248924; ENSG00000100116. [O75600-1]
ENST00000323205; ENSP00000371110; ENSG00000100116. [O75600-2]
GeneIDi23464.
KEGGihsa:23464.
UCSCiuc003atz.3. human. [O75600-1]
uc003aua.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077740 mRNA. Translation: AAC27720.1 .
AK123190 mRNA. Translation: BAC85552.1 . Frameshift.
Z97630 Genomic DNA. Translation: CAB42830.1 .
Z97630 Genomic DNA. Translation: CAX14890.1 .
BC014457 mRNA. Translation: AAH14457.1 .
CCDSi CCDS13957.1. [O75600-1 ]
CCDS54527.1. [O75600-2 ]
RefSeqi NP_001165161.1. NM_001171690.1. [O75600-2 ]
NP_055106.1. NM_014291.3. [O75600-1 ]
XP_005261467.1. XM_005261410.2. [O75600-2 ]
UniGenei Hs.54609.

3D structure databases

ProteinModelPortali O75600.
SMRi O75600. Positions 21-418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117027. 6 interactions.
IntActi O75600. 2 interactions.
STRINGi 9606.ENSP00000248924.

Chemistry

DrugBanki DB00145. Glycine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei O75600.

Proteomic databases

MaxQBi O75600.
PaxDbi O75600.
PRIDEi O75600.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248924 ; ENSP00000248924 ; ENSG00000100116 . [O75600-1 ]
ENST00000323205 ; ENSP00000371110 ; ENSG00000100116 . [O75600-2 ]
GeneIDi 23464.
KEGGi hsa:23464.
UCSCi uc003atz.3. human. [O75600-1 ]
uc003aua.2. human.

Organism-specific databases

CTDi 23464.
GeneCardsi GC22P038203.
HGNCi HGNC:4188. GCAT.
HPAi HPA020460.
MIMi 607422. gene.
neXtProti NX_O75600.
PharmGKBi PA28603.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0156.
HOGENOMi HOG000221022.
HOVERGENi HBG105208.
KOi K00639.
OMAi ICDAHGA.
OrthoDBi EOG79GT68.
PhylomeDBi O75600.
TreeFami TF105923.

Enzyme and pathway databases

UniPathwayi UPA00046 ; UER00506 .

Miscellaneous databases

GenomeRNAii 23464.
NextBioi 45781.
PROi O75600.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75600.
Bgeei O75600.
CleanExi HS_GCAT.
Genevestigatori O75600.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_00985. 2am3keto_CoA_ligase.
InterProi IPR011282. 2am3keto_CoA_ligase.
IPR001917. Aminotrans_II_pyridoxalP_BS.
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.
TIGRFAMsi TIGR01822. 2am3keto_CoA. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs."
    Edgar A.J., Polak J.M.
    Eur. J. Biochem. 267:1805-1812(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Lung.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Skin.
  5. "Nuclear translocation of 2-amino-3-ketobutyrate coenzyme A ligase by cold and osmotic stress."
    Hoshino A., Fujii H.
    Cell Stress Chaperones 12:186-191(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKBL_HUMAN
AccessioniPrimary (citable) accession number: O75600
Secondary accession number(s): E2QC23, Q6ZWF1, Q96CA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 136 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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