ID C4ZDM8_AGARV Unreviewed; 490 AA.
AC C4ZDM8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Arginine/lysine/ornithine decarboxylase {ECO:0000313|EMBL:ACR77004.1};
GN OrderedLocusNames=EUBREC_3277 {ECO:0000313|EMBL:ACR77004.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR77004.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR77004.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR77004.1; -; Genomic_DNA.
DR RefSeq; WP_012744031.1; NC_012781.1.
DR AlphaFoldDB; C4ZDM8; -.
DR STRING; 515619.EUBREC_3277; -.
DR PaxDb; 515619-EUBREC_3277; -.
DR KEGG; ere:EUBREC_3277; -.
DR HOGENOM; CLU_025925_1_1_9; -.
DR Proteomes; UP000001477; Chromosome.
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; 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; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
FT DOMAIN 3..268
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 419..457
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 490 AA; 54206 MW; DABCE091CBE8C980 CRC64;
MEKELINNSQ SNIYPFHMPG HKRRGSDIGA GLDPYAIDIT EIDNFDNLHH AEGIIKEAQA
EAAALYGAKH AYFLINGSTC GILAAISAAT KRGDKVLVAR NCHKAVYHAL YLRQLHPVFT
YPEITRTGLQ GQITEAQIRA AFDENPDIKA VVITSPTYDG VVSDVAAIAS VAHEYGALLI
VDEAHGAHFG FGGGFPQNAI ALGADAVIVS LHKTLPAFTQ TALLLLGGMR EAAVEKFLGI
YETSSPSYVL MTGIERCIHY VRDNKETAFA QLRSRLDRFY QKVSGLSHLS VVRKSDFSAD
EAYDFDESKI IIFTKEAMNG HTLLELLLKK YELQLEMAAG NYVLALASVM DTDEGFDRLA
DALIEIDSRL EKYKSDFEEF YDILKQEGVV HQFYFPVKMD TTIYQKLPAV MEMYDAYDAD
HQEVYAFKAS GKVSGAFINI YPPGIPLVVP GEIMNDKLID DVIKAVNSGL EVDGLYFDPD
ADMWKFVAVL
//
