BCAT_CAEEL
ID BCAT_CAEEL Reviewed; 415 AA.
AC P54688;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE Short=BCAT;
DE EC=2.6.1.42;
DE AltName: Full=ECA39 protein;
GN Name=bcat-1; Synonyms=eca-39, eca39; ORFNames=K02A4.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-398.
RX PubMed=8692959; DOI=10.1073/pnas.93.14.7143;
RA Schuldiner O., Eden A., Ben-Yosef T., Yanuka O., Simchen G., Benvenisty N.;
RT "ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S
RT cell cycle regulation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7143-7148(1996).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26620638; DOI=10.1038/ncomms10043;
RA Mansfeld J., Urban N., Priebe S., Groth M., Frahm C., Hartmann N.,
RA Gebauer J., Ravichandran M., Dommaschk A., Schmeisser S., Kuhlow D.,
RA Monajembashi S., Bremer-Streck S., Hemmerich P., Kiehntopf M., Zamboni N.,
RA Englert C., Guthke R., Kaleta C., Platzer M., Suehnel J., Witte O.W.,
RA Zarse K., Ristow M.;
RT "Branched-chain amino acid catabolism is a conserved regulator of
RT physiological ageing.";
RL Nat. Commun. 6:10043-10043(2015).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine.
CC {ECO:0000269|PubMed:26620638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC Evidence={ECO:0000305|PubMed:26620638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC Evidence={ECO:0000305|PubMed:26620638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC Evidence={ECO:0000305|PubMed:26620638};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expression decreases with increasing age.
CC {ECO:0000269|PubMed:26620638}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown extends mean lifespan by
CC 25% and maximum lifespan by 19%, increases maximum moving speed, and
CC increases levels of the enzyme substrates, L-leucine, L-isoleucine and
CC L-valine. {ECO:0000269|PubMed:26620638}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47236.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z67883; CAA91805.1; -; Genomic_DNA.
DR EMBL; U21550; AAC47236.1; ALT_FRAME; mRNA.
DR PIR; T23215; T23215.
DR RefSeq; NP_510144.1; NM_077743.4.
DR AlphaFoldDB; P54688; -.
DR SMR; P54688; -.
DR BioGRID; 46327; 26.
DR STRING; 6239.K02A4.1; -.
DR EPD; P54688; -.
DR PaxDb; P54688; -.
DR PeptideAtlas; P54688; -.
DR EnsemblMetazoa; K02A4.1.1; K02A4.1.1; WBGene00001149.
DR GeneID; 181423; -.
DR KEGG; cel:CELE_K02A4.1; -.
DR UCSC; K02A4.1; c. elegans.
DR CTD; 181423; -.
DR WormBase; K02A4.1; CE03457; WBGene00001149; bcat-1.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR HOGENOM; CLU_031922_0_1_1; -.
DR InParanoid; P54688; -.
DR OMA; LTEVFAC; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; P54688; -.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR PRO; PR:P54688; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001149; Expressed in larva and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006550; P:isoleucine catabolic process; IMP:UniProtKB.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IMP:UniProtKB.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR11825; PTHR11825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..415
FT /note="Branched-chain-amino-acid aminotransferase,
FT cytosolic"
FT /id="PRO_0000103296"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 86
FT /note="D -> I (in Ref. 2; AAC47236)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="F -> FS (in Ref. 2; AAC47236)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..397
FT /note="MQKFYNT -> RKILQHN (in Ref. 2; AAC47236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47342 MW; AE216FC9623FB390 CRC64;
MPAILSRVAP RTFNLVGSRL MASAARLETV PREEIHKEYD RKKTFYHRDL EIQLAGPTQL
KTKPLDPTKL KFGHTYADYM MTCDWDAERG WHHPKIEPIG ELKIHPGAKV LHYASELFEG
MKAYRGIDNK IRMFRPEMNM ARMKRTALRA ALPDFDSEEM INVLTELLRL DQEWVPNSDV
CSLYLRPTLI GTDPTLGVGC ATEAKMFVIT GPVGAYYSTG FQPVSLLADS RFIRAFPGGV
GAYKMGCNYA PTIWVGKEAA SKNCQQVLWL YGENEDLTEV GTMNIFLFWK NEEGDMELIT
PPLHRGLILP GVTRDSLLEL GREWGEYKVT ERTLNMEEVK KALSEKRLYE MFGSGTACVV
SPVGKILYHN KVTDEYEELH IPTMSSKFGV MQKFYNTIND IQYGRIIKDG WMRDI
