ILVE_PSEAE
ID ILVE_PSEAE Reviewed; 307 AA.
AC O86428;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
GN Name=ilvE; OrderedLocusNames=PA5013;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RA Franklund C.V., Coyne M.J. Jr., Goldberg J.B.;
RT "Clustering of the lipopolysaccharide core genes, waaF, waaC, waaG, and
RT waaP, in Pseudomonas aeruginosa.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 244-265.
RC STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
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; U63816; AAC33172.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08398.1; -; Genomic_DNA.
DR PIR; A83021; A83021.
DR RefSeq; NP_253700.1; NC_002516.2.
DR RefSeq; WP_003095783.1; NZ_QZGE01000002.1.
DR PDB; 6NST; X-ray; 2.14 A; A/B/C/D/E/F=1-307.
DR PDBsum; 6NST; -.
DR AlphaFoldDB; O86428; -.
DR SMR; O86428; -.
DR STRING; 287.DR97_2368; -.
DR PaxDb; O86428; -.
DR PRIDE; O86428; -.
DR EnsemblBacteria; AAG08398; AAG08398; PA5013.
DR GeneID; 881423; -.
DR KEGG; pae:PA5013; -.
DR PATRIC; fig|208964.12.peg.5253; -.
DR PseudoCAP; PA5013; -.
DR HOGENOM; CLU_020844_3_1_6; -.
DR InParanoid; O86428; -.
DR OMA; LTEVFAC; -.
DR PhylomeDB; O86428; -.
DR BioCyc; MetaCyc:MON-11691; -.
DR BioCyc; PAER208964:G1FZ6-5129-MON; -.
DR BRENDA; 2.6.1.42; 5087.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
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; Direct protein sequencing;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="Branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000103270"
FT MOD_RES 160
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 85..104
FT /note="RAAVRENNLESAYIRPMVFY -> APPCARTTWKAPISARWCST (in
FT Ref. 1; AAC33172)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> S (in Ref. 1; AAC33172)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:6NST"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:6NST"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 192..204
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6NST"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:6NST"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6NST"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6NST"
SQ SEQUENCE 307 AA; 34085 MW; 5CD5CC6CFCDE423E CRC64;
MSMADRDGVI WYDGELVQWR DATTHVLTHT LHYGMGVFEG VRAYDTPQGT AIFRLQAHTD
RLFDSAHIMN MQIPYSRDEI NEATRAAVRE NNLESAYIRP MVFYGSEGMG LRASGLKVHV
IIAAWSWGAY MGEEALQQGI KVRTSSFTRH HVNISMTRAK SNGAYINSML ALQEAISGGA
DEAMMLDPEG YVAEGSGENI FIIKDGVIYT PEVTACLNGI TRNTILTLAA EHGFKLVEKR
ITRDEVYIAD EAFFTGTAAE VTPIREVDGR KIGAGRRGPV TEKLQKAYFD LVSGKTEAHA
EWRTLVK
