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Database: UniProt
Entry: A0A2T0BB19_9CLOT
LinkDB: A0A2T0BB19_9CLOT
Original site: A0A2T0BB19_9CLOT 
ID   A0A2T0BB19_9CLOT        Unreviewed;       450 AA.
AC   A0A2T0BB19;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Putrescine aminotransferase {ECO:0000313|EMBL:PRR81007.1};
DE            EC=2.6.1.82 {ECO:0000313|EMBL:PRR81007.1};
GN   Name=patA_3 {ECO:0000313|EMBL:PRR81007.1};
GN   ORFNames=CLVI_28450 {ECO:0000313|EMBL:PRR81007.1};
OS   Clostridium vincentii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR81007.1, ECO:0000313|Proteomes:UP000239471};
RN   [1] {ECO:0000313|EMBL:PRR81007.1, ECO:0000313|Proteomes:UP000239471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR81007.1,
RC   ECO:0000313|Proteomes:UP000239471};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium vincentii DSM 10228.";
RL   Submitted (MAR-2018) 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:PRR81007.1}.
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DR   EMBL; PVXQ01000038; PRR81007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0BB19; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000239471; Unassembled WGS sequence.
DR   GO; GO:0033094; F:putrescine--2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; 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; 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; 2.
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:PRR81007.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239471};
KW   Transferase {ECO:0000313|EMBL:PRR81007.1}.
SQ   SEQUENCE   450 AA;  49606 MW;  DC61494909C527E6 CRC64;
     MNIERINEEL DRVVGYIKSP VLTTEAQDMI VRDSVDNYNE FVNPGWLKYR KSVSTDATFV
     EWRDEGEHFY DVHGEEFIDC LGGFGIFMCG HRNPEILEVV EAQLHRQALH SQELLDPLRG
     YLAKAVSAIT PGDLQYCFFT NGGAEAVEMA LKLARIATGG RWYIAAIDGF HGKSMGAISV
     GGKDTYRAPY LPMVQQVQHV EFGDADAIRK AIKNLQHVGE KVAAVVLEPI QGEAGVIIPP
     KGYLKEVRKI CDELGVCLIF DEIQTGMGRT GTMFRCEAED VVPDILTYGK AFGGGIMPIT
     GIIARPHLWI QELQDNPWIL GSPTFGGNPL ACSAALATIK YMIDNDIPAL AAEKGIHLKS
     GLQKIAEKYP EVIQEVRGIG VMIGVEFGAC ELGYAIAKGL FKRRVMTAGT LVNAKTIRFE
     PSATISHEDI DKVIIKFEEA VIDTKKEFNL
//
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