ID A0A1R1MK77_9BACT Unreviewed; 453 AA.
AC A0A1R1MK77;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:OMH40169.1};
GN ORFNames=BLW93_06610 {ECO:0000313|EMBL:OMH40169.1};
OS Desulfurobacterium indicum.
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=1914305 {ECO:0000313|EMBL:OMH40169.1, ECO:0000313|Proteomes:UP000187408};
RN [1] {ECO:0000313|EMBL:OMH40169.1, ECO:0000313|Proteomes:UP000187408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K6013 {ECO:0000313|EMBL:OMH40169.1,
RC ECO:0000313|Proteomes:UP000187408};
RA Cao J., Shao Z., Alain K., Jebbar M.;
RT "Genome sequence of a sulfur-reducing bacterium Desulfurobacterium indicum
RT K6013.";
RL Submitted (OCT-2016) 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}.
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:OMH40169.1}.
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DR EMBL; MOEN01000025; OMH40169.1; -; Genomic_DNA.
DR RefSeq; WP_076713311.1; NZ_MOEN01000025.1.
DR AlphaFoldDB; A0A1R1MK77; -.
DR STRING; 1914305.BLW93_06610; -.
DR OrthoDB; 9805604at2; -.
DR Proteomes; UP000187408; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR CDD; cd06841; PLPDE_III_MccE_like; 1.
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; 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; 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:UP000187408}.
FT DOMAIN 64..311
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 312..397
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 85
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 453 AA; 51020 MW; A20FDEFFD84CD2BA CRC64;
MKKAYEKPAI FKLHTGMMNK FGSFASPLSR KIRKEIDGVK ISELVEKFGT PLFVFSEKAL
RSKFREIKRA FTTRYPNVEF SWSYKTNYLD AICAILHDEG ETAEVVSEFE YQKARRLGVR
GNEIVFNGPY KPVDALKVAV AEGARINIDT FEEIADLEEV AAELGIKPKV AIRLNMDTGI
HPQWSRFGFN LESGQAFDAV KRIAFGGKLE LAGLHCHIGT FILEPKAYET EVRKMVDFAY
KVEDEFGFKI EYIDIGGGFP SKNRLKGVYL PPEVVVPSID EIADRICSAL LSSLRPGDFP
KLIIESGRAI VDEAGYLIAK VHATKRLPDG RKGYILDAGV NILFTAFWYH FNVEIDREVQ
GPSEPCVLYG PLCMNIDVVD ELAYLPPLPR GTNLILSPVG AYNVTQWMQF IRYRPNVVLI
GQNGEVDLIR EAETLEDIVG RERLPERLKL NGN
//
