BCA1_SCHPO
ID BCA1_SCHPO Reviewed; 427 AA.
AC O14370; O94352;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial;
DE Short=BCAT;
DE EC=2.6.1.42;
DE Flags: Precursor;
GN Name=eca39; ORFNames=SPBC428.02c, SPBC582.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX PubMed=9483807;
RX DOI=10.1002/(sici)1097-0061(19980130)14:2<189::aid-yea210>3.0.co;2-v;
RA Eden A., Benvenisty N.;
RT "Characterization of a branched-chain amino-acid aminotransferase from
RT Schizosaccharomyces pombe.";
RL Yeast 14:189-194(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine.
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:0000269|PubMed:9483807};
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:0000269|PubMed:9483807};
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:0000269|PubMed:9483807};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Nucleus
CC {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U88029; AAC39352.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAB46675.2; -; Genomic_DNA.
DR PIR; T40454; T40454.
DR RefSeq; NP_595180.2; NM_001021088.2.
DR AlphaFoldDB; O14370; -.
DR SMR; O14370; -.
DR BioGRID; 277349; 35.
DR STRING; 4896.SPBC428.02c.1; -.
DR iPTMnet; O14370; -.
DR MaxQB; O14370; -.
DR PaxDb; O14370; -.
DR PRIDE; O14370; -.
DR EnsemblFungi; SPBC428.02c.1; SPBC428.02c.1:pep; SPBC428.02c.
DR GeneID; 2540831; -.
DR KEGG; spo:SPBC428.02c; -.
DR PomBase; SPBC428.02c; eca39.
DR VEuPathDB; FungiDB:SPBC428.02c; -.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_031922_0_1_1; -.
DR InParanoid; O14370; -.
DR OMA; LTEVFAC; -.
DR BRENDA; 2.6.1.42; 5613.
DR Reactome; R-SPO-70895; Branched-chain amino acid catabolism.
DR PRO; PR:O14370; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IGI:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IGI:PomBase.
DR GO; GO:0052654; F:L-leucine transaminase activity; IGI:PomBase.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IGI:PomBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:PomBase.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IGI:PomBase.
DR GO; GO:0009098; P:leucine biosynthetic process; IGI:PomBase.
DR GO; GO:0009099; P:valine biosynthetic process; IGI:PomBase.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Mitochondrion; Nucleus;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..427
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001280"
FT MOD_RES 256
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 236..243
FT /note="VKLCCSEE -> LSFVAPKK (in Ref. 1; AAC39352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 47855 MW; 3233011479561478 CRC64;
MSLMFLRRAG NIKGRNIRFA LQRGSVGYSQ QSSEACKNFL NTTQLRTMVQ TAALHGPKPM
DSSHIKVTNV KELKPLPEWK SLKFGENFTD HMLIMKWNRE KGWSTPEIVP FGKLCFHPAS
SVFHYGFECF EGMKAFRDEK GVPRLFRPIK NAERMLSTGT RISLPSFDPA ELAEIIRKFV
AHENRWVPDQ RGYSLYIRPT FIGTDEALGV HHCDNAMLYV IASPVGPYYS SGFKAVKLCC
SEESVRAWPG GTGHYKLGGN YAPSVLPQKE AAKKGYAQIL WLYGDEDYIT EVGTMNCFTV
WINKNGEKEI ITAPLDGMIL PGVTRDSILE ICRERLAPKG WKITEGKYSM KEVAQASKEG
RLLEVFGAGT AALVSPVKAI NYKGTEYEIP MPEGQEAGPI TSEISKWILD IQYGKEPNNP
WSVPALP
