ID   A0A417UCR4_9FIRM        Unreviewed;       552 AA.
AC   A0A417UCR4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Aminotransferase class V-fold PLP-dependent enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DXB46_01990 {ECO:0000313|EMBL:RHV51507.1};
OS   Lachnospiraceae bacterium OM04-12BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=2292272 {ECO:0000313|EMBL:RHV51507.1, ECO:0000313|Proteomes:UP000284430};
RN   [1] {ECO:0000313|EMBL:RHV51507.1, ECO:0000313|Proteomes:UP000284430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM04-12BH {ECO:0000313|EMBL:RHV51507.1,
RC   ECO:0000313|Proteomes:UP000284430};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-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   -!- 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:RHV51507.1}.
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; QULQ01000002; RHV51507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A417UCR4; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000284430; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 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   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF3; LYSINE 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284430}.
FT   DOMAIN          36..338
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          452..518
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   552 AA;  62498 MW;  E528D801B4E6D437 CRC64;
     MGCHCGRQIL FPSGNPEDPE KAWQSQSGSC QMNLLAEELK RYGESDFYPF HMPGHKRKEM
     GSPVSRVYPL DITEIDGFDN LHHAEGILKE AQERAGKLYH SEKTYFLVNG STCGLLTAIS
     AVAGRGSRIL VARNCHKAVY HGIMLNHLQP EYLFPELIEA YGISGGISAK QVERSLQELV
     QRENIPEKEI SSMVCAVLVT SPSYDGILSD VRGICEAAHH YGIPVIVDQA HGAHFGFHRR
     LPESAVTEGA DLVIHSVHKM LPAPTQTALL HVNGKLVDPE LVQKYLAVYE TSSPSYLLMA
     GIDSCMAYLE KEGEAPFERI LKYRQRLTER CRDLKHIRIY PADMTEHSVE GEAGLVMDEA
     VCRRQEPFRF LISVRGSGCG GSFLMEQLRR KYHLELEMAA YDYVIALLSV MDDREGFERL
     ADALREIDLE IERQMQEPGK NPAKEKPASV SIFYQQYKPK QSYRMEEVFR AETEEVLLGD
     SDRRTAADFV MLYPPGIPVL VPGEEIDKTL IRMIREYLEQ GFDLQGITHQ NDMENDGNHY
     KIRCVKEESR RS
//