ID A0A0S8HGK1_9BACT Unreviewed; 462 AA.
AC A0A0S8HGK1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Diaminopimelate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMS25_00840 {ECO:0000313|EMBL:KPK83181.1};
OS Gemmatimonas sp. SM23_52.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK83181.1, ECO:0000313|Proteomes:UP000051975};
RN [1] {ECO:0000313|EMBL:KPK83181.1, ECO:0000313|Proteomes:UP000051975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK83181.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK83181.1}.
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DR EMBL; LJUM01000003; KPK83181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HGK1; -.
DR PATRIC; fig|1703359.3.peg.2846; -.
DR Proteomes; UP000051975; 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}.
FT DOMAIN 44..322
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 323..412
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 385
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 462 AA; 50440 MW; AA2D64CD7CB575BE CRC64;
MNLKVEDWGF EAAVDGTLLI GGLRAESLAR EFGTPLHVVD ESGLRRRAAR LRDAFEWAYS
GQVTAYYALK CNNTPGIVRM ILDEGFRPEV GTTYEWCLAR RLGAEPGEIM INGPNKGELL
RTAVAEGAGL IVVDGPQELE DLEALCRSTA RRARILLRVN PNSVPKGMNR ASATGSRKAS
VFGFDLVSGE VSRALERIAR SPSLHLAGLH CHVGTGVRRT RDYKRPLEVL VDCAAEASSY
GLKIEVINVG GGFGVPTSRE LDTLEFLLYQ GIGRLPKPPE PSRFPSVEDF AALVTDTIQR
GCERHDLALP RLVVEPGRAI VSGAGVLLLG VGAVKQRPGV GTWVITDGAA GTVGFPLYYE
YHEVFLCSAV NAPRTERYSL VGPVCFSADW IYRNKRMPQI VPGDVLAVCD AGAYFTVQET
NFGFPRPPIV VVRDGKATLL RRRETFEDMV SRDIGWNDGN EP
//
