ID R5TE22_9FIRM Unreviewed; 510 AA.
AC R5TE22;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Arginine/lysine/ornithine decarboxylases {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN683_00984 {ECO:0000313|EMBL:CCZ63903.1};
OS Roseburia sp. CAG:50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262949 {ECO:0000313|EMBL:CCZ63903.1, ECO:0000313|Proteomes:UP000018378};
RN [1] {ECO:0000313|EMBL:CCZ63903.1, ECO:0000313|Proteomes:UP000018378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:50 {ECO:0000313|Proteomes:UP000018378};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ63903.1}.
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DR EMBL; CBAK010000026; CCZ63903.1; -; Genomic_DNA.
DR AlphaFoldDB; R5TE22; -.
DR Proteomes; UP000018378; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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: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:UP000018378}.
FT DOMAIN 27..314
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 439..495
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 510 AA; 56744 MW; DA34FA0E4A36403A CRC64;
MEPKQKTEQD TTVGKEHFVQ KTEYLDEKLL AYSQTDAYPF HMPGHKRQSM GNWTGEAIDI
TEITGFDNLH HAEGILQEAQ CRAAETFGAD KTFFLINGST AGLLSAICGT VRRGGRLLMA
RNCHKAVYHA VYLMELKTAY LYPEQTDFGI QGSISPEQVR DMLEQYPDTE AVLLTSPTYD
GVVSDIAAIA ALAHEKGVPL IVDEAHGAHF GFSQGFPQKA LAFGADLCIE SVHKTLPAYT
QSALLHYRKN PWINLERVKQ YLGIYQTSSP SYILMAGIDR CTRILREQGT ELFAAYEQRL
HDFYEKCRTL QRITVLSPGG EIGENGENDP GIWARDPSKI LICAEDAGLH GQELAELLTE
HYHLELEMAS GHYATALTTL MDTQEGFDRL FAALQAIDRK NRKSGMLHQG QELETADLFT
TDDIYCEAEK VLDIAEAMDA PKTTIPLMSA AGCVSGEFVY LYPPGIPILA PGERVTEEIL
ETLRICQARN MQIEGMKDYS GQSLEICNIL
//