ID I0GU25_SELRL Unreviewed; 418 AA.
AC I0GU25;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative diaminopimelate decarboxylase {ECO:0000313|EMBL:BAL84262.1};
DE EC=4.1.1.20 {ECO:0000313|EMBL:BAL84262.1};
GN Name=lysA {ECO:0000313|EMBL:BAL84262.1};
GN OrderedLocusNames=SELR_25540 {ECO:0000313|EMBL:BAL84262.1};
OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL84262.1, ECO:0000313|Proteomes:UP000007887};
RN [1] {ECO:0000313|EMBL:BAL84262.1, ECO:0000313|Proteomes:UP000007887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT TAM6421.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
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DR EMBL; AP012292; BAL84262.1; -; Genomic_DNA.
DR RefSeq; WP_014425681.1; NC_017068.1.
DR AlphaFoldDB; I0GU25; -.
DR KEGG; sri:SELR_25540; -.
DR PATRIC; fig|927704.6.peg.2638; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_2_9; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000007887; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR CDD; cd06828; PLPDE_III_DapDC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR002986; DAP_deCOOHase_LysA.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01181; DAPDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:BAL84262.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 31..278
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 279..368
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 418 AA; 46672 MW; 8059CFC3F3C46190 CRC64;
MSKKYFPLST ERLHEVIKKF PTPFHIYEEK AIRENIRALQ AAFAWAPAFH EQFAVKALPN
PRIVQILHEE GAGTDCSSLA ELLISEAAGL KGEEILLTSN DTPADEFQKA VELGAIINLD
DITHLDYLEE HAGLPQVLCF RYNPGDAVEG NDIIGQPTEA KYGLTHDQML EGYRRAKEKG
VKRFGLHTMV ASNERRTEAF LLTARLMFEL AVELKEKLDI SVEFVNLGGG FGIPYRPEEE
PLNLKEIGEG IHQLYNEMMV PHGLDKTAIM TENGRAMTGP AGWLVSTAIH EKHTYKDYIG
LDSCMANLMR PALYGAYHHI TVAGKENAPC DHTYDVTGSL CENNDKFAID RQLPEINIGD
IVIIHDTGAH GSAMGFNYNG KLWCAELLLR EDGSIELIRR AQTIDDYFAT LKYPGSLL
//
