GenomeNet

Database: UniProt
Entry: A0A229VZS0_9BIFI
LinkDB: A0A229VZS0_9BIFI
Original site: A0A229VZS0_9BIFI 
ID   A0A229VZS0_9BIFI        Unreviewed;       457 AA.
AC   A0A229VZS0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:OXN01085.1};
GN   ORFNames=Tam10B_0664 {ECO:0000313|EMBL:OXN01085.1};
OS   Bifidobacterium vansinderenii.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1984871 {ECO:0000313|EMBL:OXN01085.1, ECO:0000313|Proteomes:UP000215433};
RN   [1] {ECO:0000313|EMBL:OXN01085.1, ECO:0000313|Proteomes:UP000215433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tam10B {ECO:0000313|EMBL:OXN01085.1,
RC   ECO:0000313|Proteomes:UP000215433};
RA   Lugli G.A., Duranti S., Mangifesta M.;
RT   "Bifidobacterium vansinderenii sp. nov.";
RL   Submitted (MAY-2017) 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:OXN01085.1}.
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; NEWD01000006; OXN01085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229VZS0; -.
DR   OrthoDB; 3246809at2; -.
DR   Proteomes; UP000215433; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   457 AA;  50320 MW;  41879D382A050AEB CRC64;
     MTTTIDEARI KELTEKEGEK LNAKLGKSHE MYDRARKHLC NGVASSYQLR DPWPIYVDRG
     QGAKMWDVDG NEYYDFNNGF GAMLQGHANP IIAEAVNDRF SKGSHFAMPD WDDVVVAEEL
     TERFGLPKWR FNNSGSESTM DAIRIARAYT HRDHIMKIFG SYHGHHDAVM ISISEDYNNI
     GDRYHLKSLP YGAGIPKATV ELTVPVPFND LDALEHRIEE MEAAGEAPAC LIMEACLMNM
     SIVPPEPGYL EGVREVTKKH GIVLIFDEVK TGLTVGPGGA TKLFGVTPDM VTIAKSLAGG
     LPSGAIGGSD EVMSVVEDGS VYQVGTFSGN PLSMAAARAS LEKVLTPAAY EHLDRMNQRL
     MDGCSAIIKK YDFPGYAQGF GAKGCVTFSP HKITDYVSFR KGQNAALNQL AWLYQANRGV
     YMAPGREEEW TLSVAHDEKA CDTYLAAFEE MAHDLAN
//
DBGET integrated database retrieval system