ID A0A087CYS2_9BIFI Unreviewed; 453 AA.
AC A0A087CYS2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:KFI88422.1};
DE EC=2.6.1.77 {ECO:0000313|EMBL:KFI88422.1};
GN ORFNames=BREU_0537 {ECO:0000313|EMBL:KFI88422.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI88422.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI88422.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI88422.1,
RC ECO:0000313|Proteomes:UP000028984};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:KFI88422.1}.
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; JGZK01000001; KFI88422.1; -; Genomic_DNA.
DR RefSeq; WP_044089185.1; NZ_JGZK01000001.1.
DR AlphaFoldDB; A0A087CYS2; -.
DR STRING; 1437610.BREU_0537; -.
DR eggNOG; COG0161; Bacteria.
DR OrthoDB; 3246809at2; -.
DR Proteomes; UP000028984; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KFI88422.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984};
KW Transferase {ECO:0000313|EMBL:KFI88422.1}.
SQ SEQUENCE 453 AA; 50004 MW; 46EEC73059EA4553 CRC64;
MSESLATKEL TGEEVAELHR EYVMQSWHKQ GEPVIPVKSA KGIYVYDYDG NKYADMSSLL
VCSNLGHELP EIVDAIKAQA DKMCFMAPAY ASEPKSKLAK MIVDLAGSDF YQRVFFTNGG
ADSNENAIKM ARMVTGRQKI FSCYRSYHGS TLGASFASGD WRRFATEAGG AAPSFVHFMN
PNMYEDGFER GKDDAKVTAV YLKRLEDQII YENPDDIAAI IMESIVGANG VILPPDGYME
GVRALCDKYG ILMICDEVMA GWCRTGKMFA WQNFDIKPDI FTFAKGVTCG YVPLGGVVVS
KTISDYFTDH VLQCGLTYSG HTLACAAGVA AVNYYVEHDV AGHVKEMEGI LKPFLEEMAA
KHKCVGESRT IGLFSAMTIV KNKETRELMS PYHTANPVMG KIMGALKDKG FLTFGRETNV
NICPPLTITA EELKAELPKV DEVLTWVDEN FCD
//
