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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 transcript 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.
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.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	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
Molecular function	glycine C-acetyltransferase activity Non-traceable author statement Ref.1. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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
	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.3

Sequences

	Sequence		Length	Mass (Da)
	O75600 [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

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: 10712613] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Lung.
[2]	"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: 10591208] [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]. Tissue: Skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF077740 mRNA. Translation: AAC27720.1. Z97630 Genomic DNA. Translation: CAB42830.1. BC014457 mRNA. Translation: AAH14457.1.
IPI	IPI00026492.
RefSeq	NP_055106.1. NM_014291.3.
UniGene	Hs.54609.
3D structure databases
ProteinModelPortal	O75600.
SMR	O75600. Positions 24-418.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75600. 2 interactions.
STRING	O75600.
PTM databases
PhosphoSite	O75600.
Proteomic databases
PRIDE	O75600.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000248924; ENSP00000248924; ENSG00000100116.
GeneID	23464.
KEGG	hsa:23464.
UCSC	uc003atz.1. human.
Organism-specific databases
CTD	23464.
GeneCards	GC22P038203.
H-InvDB	HIX0203180.
HGNC	HGNC:4188. GCAT.
HPA	HPA020460.
MIM	607422. gene.
neXtProt	NX_O75600.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09821.
GeneTree	ENSGT00530000063111.
HOVERGEN	HBG105208.
PhylomeDB	O75600.
Gene expression databases
ArrayExpress	O75600.
Bgee	O75600.
CleanEx	HS_GCAT.
Genevestigator	O75600.
GermOnline	ENSG00000100116. Homo sapiens.
Family and domain databases
InterPro	IPR011282. 2am3keto_CoA_ligase. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00639.
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.
NextBio	45781.
SOURCE	Search...

Entry information

Entry name

KBL_HUMAN

Accession

Primary (citable) accession number: O75600
Secondary accession number(s): Q96CA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 110 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.