ID A0A1H4EED9_9GAMM Unreviewed; 442 AA.
AC A0A1H4EED9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SEA83088.1};
GN ORFNames=SAMN02982996_02626 {ECO:0000313|EMBL:SEA83088.1};
OS Lonsdalea quercina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Lonsdalea.
OX NCBI_TaxID=71657 {ECO:0000313|EMBL:SEA83088.1, ECO:0000313|Proteomes:UP000187280};
RN [1] {ECO:0000313|EMBL:SEA83088.1, ECO:0000313|Proteomes:UP000187280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29281 {ECO:0000313|EMBL:SEA83088.1,
RC ECO:0000313|Proteomes:UP000187280};
RA de Groot N.N.;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNQS01000009; SEA83088.1; -; Genomic_DNA.
DR RefSeq; WP_074728957.1; NZ_FNQS01000009.1.
DR AlphaFoldDB; A0A1H4EED9; -.
DR STRING; 71657.SAMN02982996_02626; -.
DR eggNOG; COG0019; Bacteria.
DR Proteomes; UP000187280; 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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000187280}.
FT DOMAIN 38..288
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 289..383
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 62
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 442 AA; 48777 MW; 6711E63388C2D47B CRC64;
MRHSKYDSKY INKINIEGVE YNNLADAVGT PCYIYSAGQI KDDLQQLKAA LPPELHVFFS
LKANPNLSIV RLLHQQQVGC EVCSLPELET ALMAGVQPDD IIFVGPAKSY EDLRRSVELG
IHAVVVESAD ELAMLDRIAA EQDKRPRFAL RINPDFVPAK ARLVMTGKPR QFGMDESQAL
SLIAQRDAYS HLHFCGIHIY LGTRILDAEA IARNTLNILR TAEKFQLATG NELEFVDIGG
GLGIAYHDKE TPLDLALLGR LLQDPIRQFQ QRHPRARLIM ELGRFIVARS GVFMTRVRYV
KSSRGKHFAI CDGGSNCHGA AAGLGAVIRR NFRTERLGAE SPGAPQQHYD LTGPLCTPTD
IIGENMLLPT LAAGDLIGLF NSGAYGPTAS PVYFLSFGYP AEVLVDGDRA VMIRRPDDMA
HLLRQQQAEP VSLSPIRAKQ RA
//
