ID A0A024QFM9_9BACI Unreviewed; 438 AA.
AC A0A024QFM9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1 {ECO:0000313|EMBL:CDQ40980.1};
GN Name=hemL1_1 {ECO:0000313|EMBL:CDQ40980.1};
GN ORFNames=BN990_03329 {ECO:0000313|EMBL:CDQ40980.1};
OS Virgibacillus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ40980.1, ECO:0000313|Proteomes:UP000028875};
RN [1] {ECO:0000313|EMBL:CDQ40980.1, ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ40980.1,
RC ECO:0000313|Proteomes:UP000028875};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL Submitted (MAY-2014) 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:CDQ40980.1}.
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; CCDP010000002; CDQ40980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024QFM9; -.
DR STRING; 1462526.BN990_03329; -.
DR eggNOG; COG0001; Bacteria.
DR Proteomes; UP000028875; 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; IPR049704; Aminotrans_3_PPA_site.
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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000028875}.
SQ SEQUENCE 438 AA; 48661 MW; 72CAB9E6941E7CB2 CRC64;
MIKRMNQSLA YMDRAKQVMP GGVTANIKYF EPHPIVMKKG HGAYLTDVDD NEYVDYLLSY
GSLMLGHGHP VIKHAIQSQL DTSGTWLFGT PHELEADFGE KLKQYFPSME LLRYTNSGTE
ATLLALRLAA TYTGKHKIAK FEGHYHGGYD QVLLSVDPDV NEAGPAEEPL SVPASKGVGA
YHQDHTVILP FNHSYAFELL KHHRDEIGVV VLEPIQSGFI PAQKVFMEEL RRLTKDLGIV
LLFDEVKTGF RIGMGGAQGY YGIEPDLTAL GKVIGAGFPM GVVGGKREIL MESAPVKNNA
TNLSSKDVLF HSGTYNGHPM ILAAGLATIQ VLENEFDFVV MQTNELKQQL ERLFATKGIA
MQAIGIGAMF NIVFTEEKVT NYREYQIADF RLRKDLDAHL LKEGIYAKPC NRYSLSTQHG
EKEIEKTVTA VTGFLNQM
//
