ID J9ZA23_LEPFM Unreviewed; 489 AA.
AC J9ZA23;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:AFS53340.1};
GN Name=ldcC2 {ECO:0000313|EMBL:AFS53340.1};
GN OrderedLocusNames=LFML04_1110 {ECO:0000313|EMBL:AFS53340.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS53340.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS53340.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS53340.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
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; CP002919; AFS53340.1; -; Genomic_DNA.
DR RefSeq; WP_014960850.1; NC_018649.1.
DR AlphaFoldDB; J9ZA23; -.
DR STRING; 1048260.LFML04_1110; -.
DR KEGG; lfi:LFML04_1110; -.
DR PATRIC; fig|1048260.3.peg.1209; -.
DR HOGENOM; CLU_025925_2_1_0; -.
DR Proteomes; UP000006177; Chromosome.
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: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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 224..238
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
SQ SEQUENCE 489 AA; 53708 MW; 0F9B4A688A38D1E3 CRC64;
MSHLDHNRTP LFDAMVALAE SRKVSFHTPG HKSGKGISTR FRKFVGPKVF SIDLTCLDEV
DSLQKPRGVI REAQELAADI YDADQSYFLV NGTSGGNQAM LLSCLQPGEP FLTTRILHKS
AVSGMIMADA RPIFIPLQEN KKTSLLLNDQ TDSILSTMDA HPEVRTLFLT SPNYYGVTLN
LPLVTREAHK RGIRVLLDEA HGPHLHFHEA LPVSAMTAEV DMCVQSTHKI IGGMTQASIL
HAKSARIDLG RLSSTLRYLQ TTSPSYILMA SLDLARMQMA TEGRKLLGKA LDLSRRGRDR
IRKIPGLTCI DRTEVQTLSA GDNDLDETKL TIGVSGLGLT GYQVSQRLNQ EFGIQVEMAD
LMHILVIVSI GDHREDIDRL VTSLEKIAGQ SPQSSLPAYS AELQKPYSLN PGKVSPREAF
FSSHELVPLE EAEGRIAADI VTVYPPGIPL LIPGEQINRD ILDFLFTMRG TGATLDGLDP
TNTRLKVVA
//
