ID   A0A086ZI40_9BIFI        Unreviewed;       458 AA.
AC   A0A086ZI40;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:NMF02479.1};
DE   SubName: Full=Glutamate-1-semialdehyde-2,1-aminomutase {ECO:0000313|EMBL:KFI46190.1};
DE            EC=5.4.3.8 {ECO:0000313|EMBL:KFI46190.1};
GN   ORFNames=BBOU_1276 {ECO:0000313|EMBL:KFI46190.1}, HF843_04710
GN   {ECO:0000313|EMBL:NMF02479.1};
OS   Bifidobacterium boum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=78343 {ECO:0000313|EMBL:KFI46190.1, ECO:0000313|Proteomes:UP000029093};
RN   [1] {ECO:0000313|EMBL:KFI46190.1, ECO:0000313|Proteomes:UP000029093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 10736 {ECO:0000313|EMBL:KFI46190.1,
RC   ECO:0000313|Proteomes:UP000029093};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NMF02479.1, ECO:0000313|Proteomes:UP000583419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCA-130-P53-4B {ECO:0000313|EMBL:NMF02479.1,
RC   ECO:0000313|Proteomes:UP000583419};
RA   Hitch T.C.A., Wylensek D., Clavel T.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {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:KFI46190.1}.
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; JGYQ01000016; KFI46190.1; -; Genomic_DNA.
DR   EMBL; JABAGJ010000005; NMF02479.1; -; Genomic_DNA.
DR   RefSeq; WP_026502208.1; NZ_JGYQ01000016.1.
DR   AlphaFoldDB; A0A086ZI40; -.
DR   OrthoDB; 3246809at2; -.
DR   Proteomes; UP000029093; Unassembled WGS sequence.
DR   Proteomes; UP000583419; Unassembled WGS sequence.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:NMF02479.1};
KW   Isomerase {ECO:0000313|EMBL:KFI46190.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029093};
KW   Transferase {ECO:0000313|EMBL:NMF02479.1}.
SQ   SEQUENCE   458 AA;  50487 MW;  249821A8F6DF22D0 CRC64;
     MTASISESRI KELTAKEGEK LNAKLGKSRE MYNEARKHLC NGVASSYQLR DPWPIYVDHG
     SGSKLWDVDG NEYYDFHNGY GAMVQGHGNP EIGKAIAERF PKGTHFALPD EDDFVVADEL
     TQRFGLPKWR FTNSGSEATM DAIRIARAYT HRDHIMKIFG SYHGHHDAVM ISIVGDYENI
     GDKNHLKKIP YGAGIPKSLI PLTVPVPFND ADALEARIRE METDDEAPAC LIMEACLMNM
     SIVPPEPGYL EKVREITKRH GIVLIFDEVK TGLTIGPGGA TKLFGVTPDM VTMAKAISGG
     LPMGAIGGTD EVMSVVESGE VYQVGTYSGN PLCVAAARAN LEKVLTPEAY KLFDHLNNRL
     MEGCTEVIKK YDFPGYSIGF GAKGCVTFSP HKIIDYVTFK QGQRTDLNQL CWLYAANRGV
     FMTPGREEEW TLSVAHDDAA CDAYINAFAE MAHDVTAE
//