GenomeNet

Database: UniProt
Entry: N1WN66_9LEPT
LinkDB: N1WN66_9LEPT
Original site: N1WN66_9LEPT 
ID   N1WN66_9LEPT            Unreviewed;       307 AA.
AC   N1WN66;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU364094};
DE            Short=BCAT {ECO:0000256|RuleBase:RU364094};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU364094};
GN   Name=ilvE {ECO:0000256|RuleBase:RU364094,
GN   ECO:0000313|EMBL:EMY77248.1};
GN   ORFNames=LEP1GSC060_2970 {ECO:0000313|EMBL:EMY77248.1};
OS   Leptospira weilii serovar Ranarum str. ICFT.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1218598 {ECO:0000313|EMBL:EMY77248.1, ECO:0000313|Proteomes:UP000012313};
RN   [1] {ECO:0000313|EMBL:EMY77248.1, ECO:0000313|Proteomes:UP000012313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICFT {ECO:0000313|EMBL:EMY77248.1,
RC   ECO:0000313|Proteomes:UP000012313};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC       {ECO:0000256|ARBA:ARBA00003109, ECO:0000256|RuleBase:RU364094}.
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:0000256|ARBA:ARBA00000627,
CC         ECO:0000256|RuleBase:RU364094};
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:0000256|ARBA:ARBA00000995,
CC         ECO:0000256|RuleBase:RU364094};
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:0000256|ARBA:ARBA00001745,
CC         ECO:0000256|RuleBase:RU364094};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004824, ECO:0000256|RuleBase:RU364094}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000256|ARBA:ARBA00005072,
CC       ECO:0000256|RuleBase:RU364094}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931,
CC       ECO:0000256|RuleBase:RU364094}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMY77248.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AOHC02000037; EMY77248.1; -; Genomic_DNA.
DR   RefSeq; WP_003004138.1; NZ_AOHC02000037.1.
DR   AlphaFoldDB; N1WN66; -.
DR   STRING; 1218598.LEP1GSC060_2970; -.
DR   OrthoDB; 9805628at2; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000012313; Unassembled WGS sequence.
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   CDD; cd01557; BCAT_beta_family; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 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   NCBIfam; TIGR01122; ilvE_I; 1.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF4; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU364094};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU364094};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364094}.
SQ   SEQUENCE   307 AA;  35043 MW;  9F933454C72ED209 CRC64;
     MAESIKKLSY FEGKILPESE AKISIQTHAL QYGTTVFGGV RGYYDKDTDN IYLFRILDHY
     QRLINSTRIM QLKLEKTKEN LRDITIDLIR QSGYKENIYL RPFVYTSALQ LSPRFHDVPT
     ELAIYILQLN DYLDTKRGLK TMVSSWRRFD DAVIPTLSKV SGGYVNSALA KSEAVQNGFD
     EAIFLDSRGF VSEGSAENIF LVRDGKIITP GINSSLLEGI TRRSVLQIAK DNGIEVIERD
     ISRSELYIAD EVFFSGTGVQ IAWVSEIDHR KVGNSEMGPI TKKIQSLFFN LVINKEEKYK
     HWLTPVY
//
DBGET integrated database retrieval system