ILVE_ARCFU
ID ILVE_ARCFU Reviewed; 290 AA.
AC O29329;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Putative branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
DE AltName: Full=Transaminase B;
GN Name=ilvE; OrderedLocusNames=AF_0933;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000250}.
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE000782; AAB90305.1; -; Genomic_DNA.
DR PIR; E69366; E69366.
DR RefSeq; WP_010878433.1; NC_000917.1.
DR PDB; 5MQZ; X-ray; 2.10 A; A/B/C/D/E/F=1-290.
DR PDB; 5MR0; X-ray; 1.98 A; A/B/C/D/E/F=1-290.
DR PDBsum; 5MQZ; -.
DR PDBsum; 5MR0; -.
DR AlphaFoldDB; O29329; -.
DR SMR; O29329; -.
DR STRING; 224325.AF_0933; -.
DR EnsemblBacteria; AAB90305; AAB90305; AF_0933.
DR GeneID; 24794534; -.
DR KEGG; afu:AF_0933; -.
DR eggNOG; arCOG02297; Archaea.
DR HOGENOM; CLU_020844_3_0_2; -.
DR OMA; WRGSEMM; -.
DR OrthoDB; 41340at2157; -.
DR PhylomeDB; O29329; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000002199; Chromosome.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01122; ilvE_I; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Putative branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000103289"
FT MOD_RES 150
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5MR0"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 181..193
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:5MR0"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:5MR0"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:5MR0"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:5MR0"
SQ SEQUENCE 290 AA; 32366 MW; F096FF8CFC3BA273 CRC64;
MLYVYMDGEF VPENEAKVSI FDHGFLYGDG VFEGIRAYNG RVFRLKEHID RLYDSAKAID
LEIPITKEEF MEIILETLRK NNLRDAYIRP IVTRGIGDLG LDPRKCQNPS IIVITKPWGK
LYGDLYEKGL TAITVAVRRN SFDALPPNIK SLNYLNNILA KIEANAKGGD EAIFLDRNGY
VSEGSGDNIF VVKNGAITTP PTINNLRGIT REAVIEIINR LGIPFKETNI GLYDLYTADE
VFVTGTAAEI APIVVIDGRK IGDGKPGEIT RKLMEEFSKL TESEGVPIYE
