KBL_BOVIN
ID KBL_BOVIN Reviewed; 419 AA.
AC Q0P5L8; Q9N1E8; Q9T2T7; Q9T2T8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial;
DE Short=AKB ligase;
DE EC=2.3.1.29 {ECO:0000269|PubMed:8307963};
DE AltName: Full=Aminoacetone synthase;
DE AltName: Full=Glycine acetyltransferase;
DE Flags: Precursor;
GN Name=GCAT; Synonyms=AKBCL {ECO:0000303|PubMed:8307963};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 22-42 AND 245-282, PYRIDOXAL PHOSPHATE AT LYS-265,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=8307963; DOI=10.1016/s0021-9258(17)41742-x;
RA Tong H., Davis L.;
RT "2-amino-3-ketobutyrate-CoA ligase from beef liver mitochondria.
RT Purification and partial sequence.";
RL J. Biol. Chem. 269:4057-4064(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-287.
RC TISSUE=Liver;
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).
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:0000269|PubMed:8307963}.
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:0000269|PubMed:8307963};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20738;
CC Evidence={ECO:0000305|PubMed:8307963};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:8307963};
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:0000269|PubMed:8307963}.
CC Nucleus {ECO:0000250|UniProtKB:O75600}. Note=Translocates to the
CC nucleus upon cold and osmotic stress. {ECO:0000250|UniProtKB:O75600}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BC119870; AAI19871.1; -; mRNA.
DR EMBL; AF195767; AAF44353.1; -; mRNA.
DR RefSeq; NP_001068602.1; NM_001075134.1.
DR AlphaFoldDB; Q0P5L8; -.
DR SMR; Q0P5L8; -.
DR STRING; 9913.ENSBTAP00000011095; -.
DR PaxDb; Q0P5L8; -.
DR PeptideAtlas; Q0P5L8; -.
DR PRIDE; Q0P5L8; -.
DR GeneID; 319141; -.
DR KEGG; bta:319141; -.
DR CTD; 23464; -.
DR eggNOG; KOG1359; Eukaryota.
DR HOGENOM; CLU_015846_11_0_1; -.
DR InParanoid; Q0P5L8; -.
DR OrthoDB; 930001at2759; -.
DR TreeFam; TF105923; -.
DR UniPathway; UPA00046; UER00506.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Direct protein sequencing; Mitochondrion;
KW Nucleus; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8307963"
FT CHAIN 22..419
FT /note="2-amino-3-ketobutyrate coenzyme A ligase,
FT mitochondrial"
FT /id="PRO_0000283039"
FT BINDING 134..135
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 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT BINDING 206
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 231..234
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 262..265
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 295..296
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 389
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB77"
FT MOD_RES 45
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 45
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 187
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 187
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:8307963"
FT MOD_RES 326
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 368
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 383
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
FT MOD_RES 383
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88986"
SQ SEQUENCE 419 AA; 45166 MW; C1928415976C0C16 CRC64;
MWAGRVLHAA LSRAPRESRA QSALAQLRGI LEEELESIRG AGTWKSERVI TSRQGPHIHV
DGAPGGIINF CANNYLGLSS HPEVIQAGLR TLKEFGAGLS SVRFICGTQS IHKDLEAKIA
RFHQREDAIL YPSCFDANTG LFEALLTSED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD
MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICRL ASQYGALVFV DESHATGFLG
ATGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGA LVSLLRQRAR PYLFSNSLPP
AAVGCASKAL DLLMESNAIV QSMAAKTLRF RSQMEAAGFT ISGANHPICP VMLGDARLAL
NIADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP
