ILVE_THEMA
ID ILVE_THEMA Reviewed; 273 AA.
AC P74921;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Probable branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
GN Name=ilvE; OrderedLocusNames=TM_0831;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-273.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8863738; DOI=10.1016/0378-1119(96)00508-2;
RA Guipaud O., Labedan B., Forterre P.;
RT "A gyrB-like gene from the hyperthermophilic bacterion Thermotoga
RT maritima.";
RL Gene 174:121-128(1996).
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 -!- 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; AE000512; AAD35913.1; -; Genomic_DNA.
DR EMBL; U49692; AAC44497.1; -; Genomic_DNA.
DR PIR; C72328; C72328.
DR RefSeq; NP_228640.1; NC_000853.1.
DR RefSeq; WP_004080810.1; NZ_CP011107.1.
DR PDB; 3CSW; X-ray; 2.15 A; A/B/C/D=2-273.
DR PDBsum; 3CSW; -.
DR AlphaFoldDB; P74921; -.
DR SMR; P74921; -.
DR STRING; 243274.THEMA_00485; -.
DR EnsemblBacteria; AAD35913; AAD35913; TM_0831.
DR KEGG; tma:TM0831; -.
DR eggNOG; COG0115; Bacteria.
DR InParanoid; P74921; -.
DR OMA; GEVWTST; -.
DR OrthoDB; 1275805at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR EvolutionaryTrace; P74921; -.
DR Proteomes; UP000008183; 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:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
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; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 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..273
FT /note="Probable branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000103287"
FT MOD_RES 133
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 77
FT /note="A -> R (in Ref. 2; AAC44497)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 8..18
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:3CSW"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3CSW"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3CSW"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 160..174
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3CSW"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:3CSW"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:3CSW"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3CSW"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3CSW"
SQ SEQUENCE 273 AA; 31158 MW; 2162B705612E90E3 CRC64;
MLIWWRGKFR RADEISLDFS LFEKSLQGAV YETLRTYSRA PFAAYKHYTR LKRSADFFNL
PLSLSFDEFT KVLKAGADEF KQEVRIKVYL FPDSGEVLFV FSPLNIPDLE TGVEVKISNV
RRIPDLSTPP ALKITGRTDI VLARREIVDC YDVILLGLNG QVCEGSFSNV FLVKEGKLIT
PSLDSGILDG ITRENVIKLA KSLEIPVEER VVWVWELFEA DEMFLTHTSA GVVPVRRLNE
HSFFEEEPGP VTATLMENFE PFVLNLEENW VGI
