O75600 (KBL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2.
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.

Ontologies

Keywords
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-threonine catabolic process to glycine Inferred from electronic annotation. Source: UniProtKB-UniPathway biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	mitochondrion Non-traceable author statement. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glycine C-acetyltransferase activity Non-traceable author statement Ref.1. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 21	21	Mitochondrion By similarity
	Chain	22 – 419	398	2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial		PRO_0000001246
Amino acid modifications
	Modified residue	265	1	N6-(pyridoxal phosphate)lysine Probable
Natural variations
	Alternative sequence	65	1	G → GGPGTVIFPGLPLPHLSCCI HLLSFTS in isoform 2.		VSP_044607
	Natural variant	39	1	R → C. Corresponds to variant rs710187 [ dbSNP | Ensembl ].		VAR_015094
	Natural variant	100	1	S → N. Corresponds to variant rs34468367 [ dbSNP | Ensembl ].		VAR_048229
Experimental info
	Sequence conflict	387	1	R → W in AAH14457. Ref.4
Isoform 2:
	Sequence conflict	77	1	L → S in BAC85552. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: C7760699E0474821	FASTA	419	45,285
	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
	Isoform 2 [UniParc]. Checksum: 5AD82BF1119ADC87	FASTA	445	47,974
	10 20 30 40 50 60 MWPGNAWRAA LFWVPRGRRA QSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV 70 80 90 100 110 120 DGVSGGPGTV IFPGLPLPHL SCCIHLLSFT SGILNFCANN YLGLSSHPEV IQAGLQALEE 130 140 150 160 170 180 FGAGLSSVRF ICGTQSIHKN LEAKIARFHQ REDAILYPSC YDANAGLFEA LLTPEDAVLS 190 200 210 220 230 240 DELNHASIID GIRLCKAHKY RYRHLDMADL EAKLQEAQKH RLRLVATDGA FSMDGDIAPL 250 260 270 280 290 300 QEICCLASRY GALVFMDECH ATGFLGPTGR GTDELLGVMD QVTIINSTLG KALGGASGGY 310 320 330 340 350 360 TTGPGPLVSL LRQRARPYLF SNSLPPAVVG CASKALDLLM GSNTIVQSMA AKTQRFRSKM 370 380 390 400 410 420 EAAGFTISGA SHPICPVMLG DARLASRMAD DMLKRGIFVI GFSYPVVPKG KARIRVQISA 430 440 VHSEEDIDRC VEAFVEVGRL HGALP

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
IPI	IPI00026492. IPI00446745. IPI00879060.
RefSeq	NP_001165161.1. NM_001171690.1. NP_055106.1. NM_014291.3.
UniGene	Hs.54609.
3D structure databases
ProteinModelPortal	O75600.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75600. 2 interactions.
STRING	9606.ENSP00000248924.
PTM databases
PhosphoSite	O75600.
Proteomic databases
PaxDb	O75600.
PRIDE	O75600.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000248924; ENSP00000248924; ENSG00000100116. ENST00000323205; ENSP00000371110; ENSG00000100116.
GeneID	23464.
KEGG	hsa:23464.
UCSC	uc003atz.3. human.
Organism-specific databases
CTD	23464.
GeneCards	GC22P038203.
HGNC	HGNC:4188. GCAT.
HPA	HPA020460.
MIM	607422. gene.
neXtProt	NX_O75600.
PharmGKB	PA28603.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0156.
HOGENOM	HOG000221022.
HOVERGEN	HBG105208.
KO	K00639.
OMA	EICCLAS.
PhylomeDB	O75600.
Enzyme and pathway databases
UniPathway	UPA00046; UER00506.
Gene expression databases
ArrayExpress	O75600.
Bgee	O75600.
CleanEx	HS_GCAT.
Genevestigator	O75600.
GermOnline	ENSG00000100116. Homo sapiens.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	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]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01822. 2am3keto_CoA. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00145. Glycine. DB00114. Pyridoxal Phosphate.
GenomeRNAi	23464.
NextBio	45781.
SOURCE	Search...

Entry information

Entry name

KBL_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 123 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.