ID A0A238Y298_9ACTN Unreviewed; 436 AA.
AC A0A238Y298;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SNR64694.1};
GN ORFNames=SAMN06272737_11712 {ECO:0000313|EMBL:SNR64694.1};
OS Blastococcus mobilis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1938746 {ECO:0000313|EMBL:SNR64694.1, ECO:0000313|Proteomes:UP000198403};
RN [1] {ECO:0000313|EMBL:SNR64694.1, ECO:0000313|Proteomes:UP000198403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44272 {ECO:0000313|EMBL:SNR64694.1,
RC ECO:0000313|Proteomes:UP000198403};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNO01000017; SNR64694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238Y298; -.
DR Proteomes; UP000198403; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
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; 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.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000198403}.
FT DOMAIN 41..393
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 51..295
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 70
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 436 AA; 45298 MW; 731CBFAE46CEA1E8 CRC64;
MLSPPSAAGT DCAHVLPPTA LPPAIRHLLH ARTRAETVSG YVYDPRVAAA RARALRAVLP
PWASLFFAAK ANGFPAVLAA LAGSGGVDGF EVASRAEADA ARAALLAAGR SPRLLAAGPA
KAPALLDALL DAGTEVVHVE SPLELVRLSA VAQARGRTVR VGLRVNPAAV GVRGTLAMGG
RPAPFGVPEP DVPEVLALAR SLPGLDVAGF HVHAVCGNRD ARAHAAYVGW CLDWAARTAR
QHGVDLRWVD VGGGLGVAYG GEDPLDVDLL GEELHRLTPP AGVEVALEPG RWLVADCGWY
AAEVVDVKHS YGTAYVLVRG GIGGFALPGT EDFPFALTVL PVEDWPSALP RPELRDVPVT
VVGELCTPED VLVRDVVVNR VRAGDLVVIP QAGAYGWEFA LQSFLGHPPA TRDVVVPGAD
IPPAPPVLAP VLEVVP
//
