ID A0A2B2CBG6_9BACI Unreviewed; 457 AA.
AC A0A2B2CBG6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putrescine aminotransferase {ECO:0000313|EMBL:PFP29571.1};
GN ORFNames=COJ96_10545 {ECO:0000313|EMBL:PFP29571.1};
OS Bacillus sp. AFS073361.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP29571.1, ECO:0000313|Proteomes:UP000223997};
RN [1] {ECO:0000313|EMBL:PFP29571.1, ECO:0000313|Proteomes:UP000223997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS073361 {ECO:0000313|EMBL:PFP29571.1,
RC ECO:0000313|Proteomes:UP000223997};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-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:PFP29571.1}.
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DR EMBL; NUZU01000015; PFP29571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B2CBG6; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000223997; 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; 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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF112; PUTRESCINE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:PFP29571.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000223997};
KW Transferase {ECO:0000313|EMBL:PFP29571.1}.
SQ SEQUENCE 457 AA; 50346 MW; 4FCD23750E2725D0 CRC64;
MSIDLKNELK SEQNQKVSEY INKVLNLIEK EEINSEEAAW ITKETVDGFR EHVNPGFLEY
RKTVTEGGQF AAVEWSDNGS CFKDVNGKEY IDCLGGFGIY NVGHRNPKVV KAVTDQLKRQ
ALHSQDLLDP LRAMLAKILA DITPGDLKYA FFTNSGTESV EASLKLAKMY SERTTFISTT
RAFHGKSLGS LSGTAKGMFR KPFLPLIPGF RHVPFGDIDM MRKTFEVCAS VGEDVAAVLL
EPIQGEGGII LPPENYLKQV RELCDQYGSL LIFDEVQTGM GRTGKMFAAE LYEVVPDIIC
LAKAFGGGVM PAGAVVASEK VFKSWFDNPF MHTTTFGGNP LACAAAIATI GVLIEDKLPE
RAAEVGAYFL EELKKAAQGH ENRVQEIRGQ GLMIGIEFHQ DEIGYEVSKG MFDRGILVAG
TLINSKTIRI EPALTISYKE VNKVVSTFKT VLEQLEA
//
