KBL_MOUSE
ID KBL_MOUSE Reviewed; 416 AA.
AC O88986;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial;
DE Short=AKB ligase;
DE EC=2.3.1.29 {ECO:0000250|UniProtKB:Q0P5L8};
DE AltName: Full=Aminoacetone synthase;
DE AltName: Full=Glycine acetyltransferase;
DE Flags: Precursor;
GN Name=Gcat; Synonyms=Kbl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=10712613; DOI=10.1046/j.1432-1327.2000.01175.x;
RA Edgar A.J., Polak J.M.;
RT "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme
RT A ligase cDNAs.";
RL Eur. J. Biochem. 267:1805-1812(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-184; LYS-323; LYS-365
RP AND LYS-380, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-184 AND LYS-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=29323231; DOI=10.1038/s41598-017-18828-3;
RA Tani H., Ohnishi S., Shitara H., Mito T., Yamaguchi M., Yonekawa H.,
RA Hashizume O., Ishikawa K., Nakada K., Hayashi J.I.;
RT "Mice deficient in the Shmt2 gene have mitochondrial respiration defects
RT and are embryonic lethal.";
RL Sci. Rep. 8:425-425(2018).
CC -!- FUNCTION: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes
CC the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA.
CC Catalyzes the second reaction step on the main metabolic degradation
CC pathway for L-threonine. {ECO:0000250|UniProtKB:Q0P5L8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA;
CC Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29;
CC Evidence={ECO:0000250|UniProtKB:Q0P5L8};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20738;
CC Evidence={ECO:0000250|UniProtKB:Q0P5L8};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q0P5L8};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC reductase pathway; glycine from L-threonine: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}.
CC Nucleus {ECO:0000250|UniProtKB:O75600}. Note=Translocates to the
CC nucleus upon cold and osmotic stress. {ECO:0000250|UniProtKB:O75600}.
CC -!- DEVELOPMENTAL STAGE: Present in the placenta, brain and liver during
CC embryonic development (at protein level).
CC {ECO:0000269|PubMed:29323231}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:29323231}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF093403; AAC99774.1; -; mRNA.
DR EMBL; AK087433; BAC39872.1; -; mRNA.
DR EMBL; BC024107; AAH24107.1; -; mRNA.
DR CCDS; CCDS27630.1; -.
DR RefSeq; NP_038875.3; NM_013847.4.
DR AlphaFoldDB; O88986; -.
DR SMR; O88986; -.
DR BioGRID; 205059; 3.
DR STRING; 10090.ENSMUSP00000006544; -.
DR iPTMnet; O88986; -.
DR PhosphoSitePlus; O88986; -.
DR SwissPalm; O88986; -.
DR REPRODUCTION-2DPAGE; O88986; -.
DR SWISS-2DPAGE; O88986; -.
DR EPD; O88986; -.
DR jPOST; O88986; -.
DR MaxQB; O88986; -.
DR PaxDb; O88986; -.
DR PeptideAtlas; O88986; -.
DR PRIDE; O88986; -.
DR ProteomicsDB; 263575; -.
DR DNASU; 26912; -.
DR Ensembl; ENSMUST00000006544; ENSMUSP00000006544; ENSMUSG00000006378.
DR GeneID; 26912; -.
DR KEGG; mmu:26912; -.
DR UCSC; uc007wse.2; mouse.
DR CTD; 23464; -.
DR MGI; MGI:1349389; Gcat.
DR VEuPathDB; HostDB:ENSMUSG00000006378; -.
DR eggNOG; KOG1359; Eukaryota.
DR GeneTree; ENSGT00940000155729; -.
DR HOGENOM; CLU_015846_11_0_1; -.
DR InParanoid; O88986; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 930001at2759; -.
DR PhylomeDB; O88986; -.
DR TreeFam; TF105923; -.
DR UniPathway; UPA00046; UER00506.
DR BioGRID-ORCS; 26912; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Gcat; mouse.
DR PRO; PR:O88986; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O88986; protein.
DR Bgee; ENSMUSG00000006378; Expressed in mammary bud and 235 other tissues.
DR ExpressionAtlas; O88986; baseline and differential.
DR Genevisible; O88986; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR InterPro; IPR011282; 2am3keto_CoA_ligase.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01822; 2am3keto_CoA; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Mitochondrion; Nucleus; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q0P5L8"
FT CHAIN 19..416
FT /note="2-amino-3-ketobutyrate coenzyme A ligase,
FT mitochondrial"
FT /id="PRO_0000001247"
FT BINDING 131..132
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 203
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 259..262
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 292..293
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT MOD_RES 42
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 42
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 184
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 184
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 262
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q0P5L8"
FT MOD_RES 323
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 365
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 380
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 380
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 416 AA; 44931 MW; 01EA71B3846BEBBF CRC64;
MWASFMWHGA LSPGRRAHSA LAQLRCILDS ELEGIRGAGT WKSERVITSR QGPSIRVDGI
SGGILNFCAN NYLGLSSHPA VIQAGLQTLE EFGAGLSSTR FICGTQSIHK NLEAKIAHFH
QREDAILYPS CFDANAGLFE ALLTPEDAVL SDELNHASII DGIRLCKAHK YRYRHLDMAD
LEAKLKEAQK HRLRLVATDG AFSMDGDIAP LQDICRLAAQ YGALVFVDEC HATGFLGPTG
RGTDELLGVM DQVTIINSTL GKALGGASGG YTTGPEPLVS LLRQRSRPYL FSNSLPPAVV
GCASKALDLL MESNAIIQSM AAKTRRFRSK MEAAGFTVSG ADHPICPVML GDARLSSQMA
DDMLKKGIFV IGFSYPVVPK GKARIRVQIS AVHSEEDIDR CVEAFVEVGR LHGALP
