ID A0A371J8M0_9FIRM Unreviewed; 471 AA.
AC A0A371J8M0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RDY29084.1};
GN ORFNames=CG710_018770 {ECO:0000313|EMBL:RDY29084.1};
OS Lachnotalea glycerini.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY29084.1, ECO:0000313|Proteomes:UP000216411};
RN [1] {ECO:0000313|EMBL:RDY29084.1, ECO:0000313|Proteomes:UP000216411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY29084.1,
RC ECO:0000313|Proteomes:UP000216411};
RX PubMed=29051240;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT glycerini Isolated from Water in Quebec City, Canada.";
RL Genome Announc. 5:e01059-17(2017).
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:RDY29084.1}.
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DR EMBL; NOKA02000072; RDY29084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371J8M0; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000216411; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 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 Aminotransferase {ECO:0000313|EMBL:RDY29084.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000216411};
KW Transferase {ECO:0000313|EMBL:RDY29084.1}.
FT DOMAIN 4..310
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 397..438
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 471 AA; 53664 MW; 2096D5CF24CD498E CRC64;
MLSLYELLKE YDESNYYPFH MPGHKRNLFN KFINPFQIDI TEIDGFDNLH HSEGILLEAQ
KRAAKLYHSE ESYFLINGTT VGLLSAISAC TTKGGTILIA RNCHKAVYNG IFLNELNSIY
SYPQNSLKYC VNCGLNPENI KQMLINNKNI QTVVITSPTY DGIVSDIESI AREVHKFNIP
LIVDEAHGAH FGFHPYFPYN SIKMGADIVV HSVHKTLPSL TQTALIHVNG TIVDREKLKK
YLNIYQTSSP SYLLMASIDY CINLIDNKGK DLFREYVDRL IYLRSELSKL KKIEIVDESI
VGHNSIFGLD RSKLIISVKN TDITGMDLYK RLLNQYHLQM EMAAGDYVLG MTSIMDSMEG
FQRLIDALIE IDKSINYVDS NYDFNSCLES EIYYSIAEAQ KQEAVKCNIE YAKGRISAEY
MYLYPPGVPL LVPGEVISGN LIRNVREYKK QGLSIEGMLD EENQIIQVIK E
//
