ID A0A1M6UGV7_9FIRM Unreviewed; 490 AA.
AC A0A1M6UGV7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:SHK68454.1};
GN ORFNames=SAMN02745123_02754 {ECO:0000313|EMBL:SHK68454.1};
OS Desulforamulus aeronauticus DSM 10349.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121421 {ECO:0000313|EMBL:SHK68454.1, ECO:0000313|Proteomes:UP000183997};
RN [1] {ECO:0000313|EMBL:SHK68454.1, ECO:0000313|Proteomes:UP000183997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10349 {ECO:0000313|EMBL:SHK68454.1,
RC ECO:0000313|Proteomes:UP000183997};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRAR01000020; SHK68454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6UGV7; -.
DR STRING; 1121421.SAMN02745123_02754; -.
DR Proteomes; UP000183997; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 1.
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: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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 5..367
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 407..481
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 490 AA; 53711 MW; 26E8590E988C6877 CRC64;
MSQKTPIIDA LEKYSNDRTI RFHMPGHKGS KTANSKAMSL LGSQAFAADV TNVPGMDDLH
QPHGVIRESQ DLAAATFGAD KTYFLINGSS CGLQALVMAT CNPGEKILVP RNIHRSILSG
IILSGAIPVF FLPEYDYEYG IPLGISPESI ENCLKVHQDA RAVLVVYPTY QGVASDIEAI
ARIVHKYNIP LLVDEAHGPH FGFHEALPKT ALEAGADASV HGTHKMLTSF TQASMLHVKG
KRINRQRLEA TLKILQSTST SYLLLASLDG ARAQMDCQGR EFVQQAIDTA MLLRGEIKKL
SNYQVLGEEL LGKPGVFAID PTKINIGLNK LMISGLWAEQ WLRKTYHIQV EMADIFNLLL
LVTSGNTASE ASYLLQALGK LSDYVESNNE LTKAYSDIRG INPFPYIPEL AMSPREAFLG
SATPLSLDEA EGAIGAEVIT CYPPGIPVIC PGERFTSEII RYLKAMKELG IHFQGCYDTE
LETVLIIKDY
//