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O75600 (KBL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial

Short name=AKB ligase
EC=2.3.1.29
Alternative name(s):
Aminoacetone synthase
Glycine acetyltransferase
Gene names
Name:GCAT
Synonyms:KBL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate. HAMAP-Rule MF_00985

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00985

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2. HAMAP-Rule MF_00985

Subcellular location

Mitochondrion By similarity. Nucleus. Note: Translocates to the nucleus upon cold and osmotic stress. Ref.5

Tissue specificity

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

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75600-1)

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: O75600-2)

The sequence of this isoform differs from the canonical sequence as follows:
     65-65: G → GGPGTVIFPGLPLPHLSCCIHLLSFTS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion By similarity
Chain22 – 4193982-amino-3-ketobutyrate coenzyme A ligase, mitochondrial HAMAP-Rule MF_00985
PRO_0000001246

Regions

Region134 – 1352Pyridoxal phosphate binding By similarity
Region262 – 2654Pyridoxal phosphate binding By similarity
Region295 – 2962Pyridoxal phosphate binding; shared with dimeric partner By similarity

Sites

Binding site1591Substrate By similarity
Binding site2061Pyridoxal phosphate By similarity
Binding site3891Substrate By similarity

Amino acid modifications

Modified residue451N6-acetyllysine; alternate By similarity
Modified residue451N6-succinyllysine; alternate By similarity
Modified residue1871N6-acetyllysine; alternate By similarity
Modified residue1871N6-succinyllysine; alternate By similarity
Modified residue2651N6-(pyridoxal phosphate)lysine Probable
Modified residue3261N6-succinyllysine By similarity
Modified residue3681N6-succinyllysine By similarity
Modified residue3831N6-acetyllysine; alternate By similarity
Modified residue3831N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence651G → GGPGTVIFPGLPLPHLSCCI HLLSFTS in isoform 2.
VSP_044607
Natural variant391R → C.
Corresponds to variant rs710187 [ dbSNP | Ensembl ].
VAR_015094
Natural variant1001S → N.
Corresponds to variant rs34468367 [ dbSNP | Ensembl ].
VAR_048229

Experimental info

Sequence conflict3871R → W in AAH14457. Ref.4
Isoform 2:
Sequence conflict771L → S in BAC85552. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C7760699E0474821

FASTA41945,285
        10         20         30         40         50         60 
MWPGNAWRAA LFWVPRGRRA QSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV 

        70         80         90        100        110        120 
DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA 

       130        140        150        160        170        180 
RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD 

       190        200        210        220        230        240 
MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG 

       250        260        270        280        290        300 
PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP 

       310        320        330        340        350        360 
AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS 

       370        380        390        400        410 
RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP 

« Hide

Isoform 2 [UniParc].

Checksum: 5AD82BF1119ADC87
Show »

FASTA44547,974

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001165161.1. NM_001171690.1.
NP_055106.1. NM_014291.3.
XP_005261467.1. XM_005261410.2.
UniGeneHs.54609.

3D structure databases

ProteinModelPortalO75600.
SMRO75600. Positions 21-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117027. 6 interactions.
IntActO75600. 2 interactions.
STRING9606.ENSP00000248924.

Chemistry

DrugBankDB00145. Glycine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteO75600.

Proteomic databases

PaxDbO75600.
PRIDEO75600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248924; ENSP00000248924; ENSG00000100116. [O75600-1]
ENST00000323205; ENSP00000371110; ENSG00000100116. [O75600-2]
GeneID23464.
KEGGhsa:23464.
UCSCuc003atz.3. human. [O75600-1]
uc003aua.2. human.

Organism-specific databases

CTD23464.
GeneCardsGC22P038203.
HGNCHGNC:4188. GCAT.
HPAHPA020460.
MIM607422. gene.
neXtProtNX_O75600.
PharmGKBPA28603.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221022.
HOVERGENHBG105208.
KOK00639.
OMAPLQEICC.
OrthoDBEOG79GT68.
PhylomeDBO75600.
TreeFamTF105923.

Enzyme and pathway databases

UniPathwayUPA00046; UER00506.

Gene expression databases

ArrayExpressO75600.
BgeeO75600.
CleanExHS_GCAT.
GenevestigatorO75600.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00985. 2am3keto_CoA_ligase.
InterProIPR011282. 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]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01822. 2am3keto_CoA. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23464.
NextBio45781.
PROO75600.
SOURCESearch...

Entry information

Entry nameKBL_HUMAN
AccessionPrimary (citable) accession number: O75600
Secondary accession number(s): E2QC23, Q6ZWF1, Q96CA9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM