ID C6BAT2_RHILS Unreviewed; 387 AA.
AC C6BAT2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=aspartate transaminase {ECO:0000256|ARBA:ARBA00012753};
DE EC=2.6.1.1 {ECO:0000256|ARBA:ARBA00012753};
GN OrderedLocusNames=Rleg_6440 {ECO:0000313|EMBL:ACS61190.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OG Plasmid pR132505 {ECO:0000313|EMBL:ACS61190.1,
OG ECO:0000313|Proteomes:UP000002256}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS61190.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS61190.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS61190.1,
RC ECO:0000313|Proteomes:UP000002256};
RC PLASMID=Plasmid pR132505 {ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000984};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CP001627; ACS61190.1; -; Genomic_DNA.
DR RefSeq; WP_012760689.1; NC_012854.1.
DR AlphaFoldDB; C6BAT2; -.
DR KEGG; rlg:Rleg_6440; -.
DR HOGENOM; CLU_017584_4_1_5; -.
DR OrthoDB; 9766084at2; -.
DR Proteomes; UP000002256; Plasmid pR132505.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACS61190.1};
KW Plasmid {ECO:0000313|EMBL:ACS61190.1};
KW Transferase {ECO:0000313|EMBL:ACS61190.1}.
FT DOMAIN 36..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 387 AA; 41295 MW; F58CE44E438521D4 CRC64;
MIAAKPNSLV ARLSAPPIPS VVAWSHEYKG GKGPLIDLSQ AVPGYPAHPE MLRLLAEAAG
QQAMTGYGPI EGEPLLRKTY AAHVAEYYGA DLSAGNIHIT AGCNQAFMCS AIALAGAGDT
VALTNPFYFN HDTTLSMLGI GRRLVDCDPA FGFLPDPGSA EAALAAGAKM LAVVTPNNPT
GAVYPPSLLH ELFVLCRRYG AWLILDETYR DFLGEDNGRP HSLLSEPGWE DTLVLLYSFS
KSFCIPGHRL GAITAGPKLI AEIAKVMDNM QICAPRSAQI AVASAIPALA DWRAGNRLEI
ARRADALRLV LSGLPDWEIG AIGAYFAFVR HPHADRSSSE VAEKLAKESG IVCLPGAYFG
EGQERYLRLA FANADVASIG LLSERLR
//
