ID G8NRB8_GRAMM Unreviewed; 814 AA.
AC G8NRB8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:AEU36196.1};
DE EC=4.1.1.18 {ECO:0000313|EMBL:AEU36196.1};
GN OrderedLocusNames=AciX8_1860 {ECO:0000313|EMBL:AEU36196.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU36196.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU36196.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; CP003130; AEU36196.1; -; Genomic_DNA.
DR RefSeq; WP_014265075.1; NC_016631.1.
DR AlphaFoldDB; G8NRB8; -.
DR STRING; 682795.AciX8_1860; -.
DR KEGG; gma:AciX8_1860; -.
DR eggNOG; COG1982; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_014292_3_0_0; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR005308; OKR_de-COase_N.
DR InterPro; IPR011193; Orn/lys/arg_de-COase.
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 InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR Pfam; PF01276; OKR_DC_1; 1.
DR Pfam; PF03711; OKR_DC_1_C; 1.
DR Pfam; PF03709; OKR_DC_1_N; 1.
DR PIRSF; PIRSF009393; Orn_decarb; 1.
DR SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AEU36196.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113}.
FT DOMAIN 21..139
FT /note="Orn/Lys/Arg decarboxylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03709"
FT DOMAIN 145..598
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 624..753
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
FT REGION 766..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 391
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 814 AA; 90868 MW; 41E628BEABF2EB74 CRC64;
MSEGRWVLLI ASEVGGTDSV SDRAMERLVE AIGKEGYEVV RTSTPEDGLS LVTSDPSHSA
ILLDWDLEGE NQFDERAALK ILRAVRRRNK KIPIFLIADR TLVSELPLEV VKQVHEYIHL
FGDTPAFIAN RVDFAVERYH EQLLPPYFRE LKKYTDQGAY SWDAPGHMGG VAYLKHPIGM
EFHKFFGENI MRSDLGISTS PLGSWLDHIG PPGESERNAA RIFGADWTFF VLGGSSTSNQ
IVGHGVIAQD DIVLADANCH KSICHSLTIT GARPVYFKPT RNGYGMIGLV PIKRFSPENV
QALIDKSPFC AGAPVKKATY AVVTNSTYDG LCYDVNRVVE ELAKSVPRIH FDEAWYAYAK
FHEIYRGRFA MGVPDEIPDR PTIFSVQSTH KMLAAFSMAS MVHIKLSQRA PLDYDQFNES
FMMHGTTSPF YPLIASLDVA AAMMDEPAGP TLMSETLQDA ISFRKAMSSV AHRLRAAEQG
WFFRLYQPEY VFDPLDGETY LFEEAADGLL TNRSSCWTLK PGEDWHGYQD EDIADDYCML
DPSKVTILTP GVNAQGVVSD WGIPAAILTE FLDGRRVEIA RTGDYTVLVL FSVGTSKGKW
GALLENLFEF KRLYDSEAPL EEALPELVLK YPARYRNVTL KELSDEMHMV MQQLNLSGLV
NAACDEDFDP VLTPAQTYQK LLRGETEKIK FSEMAGRIAA VMLVPYPPGI PMSMPGERLG
GPESPVIRLI MAMEEFGKRF PGFERETHGI EADANGEYWM RAVIETPNGK RNGRNKQRPP
SSAPPVKRRK KTIPLPGDDS PLEPGAPVKI SPER
//
