ID   A0A3S8RQ57_9BACL        Unreviewed;       490 AA.
AC   A0A3S8RQ57;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:AZK45096.1};
GN   ORFNames=EIM92_01875 {ECO:0000313|EMBL:AZK45096.1};
OS   Paenibacillus lentus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1338368 {ECO:0000313|EMBL:AZK45096.1, ECO:0000313|Proteomes:UP000273145};
RN   [1] {ECO:0000313|EMBL:AZK45096.1, ECO:0000313|Proteomes:UP000273145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25539 {ECO:0000313|EMBL:AZK45096.1,
RC   ECO:0000313|Proteomes:UP000273145};
RA   Kook J.-K., Park S.-N., Lim Y.K.;
RT   "Genome sequencing of Paenibacillus lentus DSM25539(T).";
RL   Submitted (NOV-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 Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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; CP034248; AZK45096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S8RQ57; -.
DR   KEGG; plen:EIM92_01875; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000273145; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AZK45096.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273145};
KW   Transferase {ECO:0000313|EMBL:AZK45096.1}.
FT   DOMAIN          221..235
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   490 AA;  53573 MW;  774454A0B4254A01 CRC64;
     MVHHRTPLFT ALTEHAKRNP IPFHIPGHKK GEGMENGFKT FLGDNALSID LINIAPLDDL
     HQPTGVIDEA QRLAAYAFGA DYSLFSVQGT STAIMTMIMS VCGPGDKIIV PRNLHKSILS
     AIIFAGAKPI FVAPERDADL GIDHGISVRS VKKAIERHPD AKAVLVINPT YFGVCTNLKA
     IVDLAHHYGI PVLVDEAHGA LLHFHDKLPL SAMQAGADLA ATSMHKLGGS LTQSSLLHIK
     KGIVQPEKVQ AMFSMLTTTS TSYILLASLD AARKQLALQG CEMSSKAIRL AEYARNRINE
     IPGLSSFGRE ILWTDAAFDF DPTKLTVHVR ELGITGYDAE QWLRDHYNIE VELSDLYNIL
     CLITPGDSKE AIDCLLNALA ELANEHYKQQ ADLQAVDVKL PEIPQLALTP RDAFYGDVEL
     IPIAQSAGRI IAESIYVYPP GIPILLPGEV IAEQHIRYIL EHLEVGLPVK GPEDLTVQNV
     KVVVEVKAIF
//