ID A0A1M4Z6G0_9THEO Unreviewed; 488 AA.
AC A0A1M4Z6G0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:SHF13663.1};
GN ORFNames=SAMN02746089_01368 {ECO:0000313|EMBL:SHF13663.1};
OS Caldanaerobius fijiensis DSM 17918.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobius.
OX NCBI_TaxID=1121256 {ECO:0000313|EMBL:SHF13663.1, ECO:0000313|Proteomes:UP000184088};
RN [1] {ECO:0000313|EMBL:SHF13663.1, ECO:0000313|Proteomes:UP000184088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17918 {ECO:0000313|EMBL:SHF13663.1,
RC ECO:0000313|Proteomes:UP000184088};
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; FQVH01000012; SHF13663.1; -; Genomic_DNA.
DR RefSeq; WP_073343176.1; NZ_FQVH01000012.1.
DR AlphaFoldDB; A0A1M4Z6G0; -.
DR STRING; 1121256.SAMN02746089_01368; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000184088; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184088}.
FT DOMAIN 9..322
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 388..468
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 488 AA; 53256 MW; 1B4F3160D54BB2DF CRC64;
MQKFDQNRTP LFDALKRYRE RQTVAFHVPG HKHGKGLKEF TDYVGENLMW LDVNGMEDLD
NVCNPVGVIK ETQQLAAEAF GADYAYFLVN GTSSGVQAMI MSACEPGDEI IIPRNAHKST
IGGIILSGAI PVYIQPEINH ELGIAMGVSV SSVKAAIEAH PYAKAVFIIN PTYYGVASDL
KTIVDLAHEN DMMVLVDEAH GAHLGFHPDL PISAMMAGAD MSAVSLHKTG GSMTQSSMLL
LKGNRLDPGY VKSVLNLTQT TSASYVLMAS LDVARKQLAT KGREMLEEVL RLSRIARDKI
NQIPGLRAFG KEVTGTPGSF AFDETKLGVN VMGLGLTGFE VESLLRKRYD IQVEMADLYN
ILAIVSLGDD ETSIAKLVEG LRGIAADHAG HTIKNATRSP IMPDLIVSPR DAYYSRKKVV
KLEDAEGEIS GEMVMAYPPG IPVICPGERI TAEIIDYIKA LKNEKCQLQG TEDPYADYIK
VLGQDYYN
//