ID A0A285L7R2_9NOCA Unreviewed; 744 AA.
AC A0A285L7R2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SNY80914.1};
GN ORFNames=SAMN04244553_2489 {ECO:0000313|EMBL:SNY80914.1};
OS Nocardia amikacinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY80914.1, ECO:0000313|Proteomes:UP000219565};
RN [1] {ECO:0000313|EMBL:SNY80914.1, ECO:0000313|Proteomes:UP000219565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY80914.1,
RC ECO:0000313|Proteomes:UP000219565};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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};
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DR EMBL; OBEG01000002; SNY80914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285L7R2; -.
DR STRING; 1379680.GCA_001612615_02749; -.
DR Proteomes; UP000219565; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_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 PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000219565}.
FT DOMAIN 345..544
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT REGION 26..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 678
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 368
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 744 AA; 78441 MW; 27CB6D02543D7078 CRC64;
MGLEAAVEPE LVDHDAMVLF DVAAPGKAKG GARASRSREL PVPTAPSDTT APHTGTETLE
QMTSPEADAS PREVEPAPPA AEASPLDTDT QTVEPTAPPF EAEAAHRHSG APPAEISSPR
DAGSPPLDAE AAALGTDTAP LGVDSAPLEA TTTPGHPDAP ISKNAKASPL GTGAHGVGDV
MSPSEAEAAA LDPDTAPLGA QPSPWKTSAT LLHTDAPYPA DTEASALDEA ASLRADMPFT
TEAETEYDEP ESTTDDTLAH TPNDFGDYPE PDWDDTDSDD AFLELLVEEI AGDPADRAPG
IVAPPMPAHI DEWERRVLAD PHLLDDIAFA VGGPFHLMYP ARVGENIRGF RDAFARAGVD
GLVYYGKKAN KAACVARACA ENGAGVDVSS VGELTAALAA GVRGGELMVT GPAKSDDLLW
LAVRHGALIA VDSLGELDRL AAIASAATPA RVLLRVLPAG SASRFGMTED ELDRAQSVIA
ASGPRGLEPV QLEGFSFHLS GYDAIARAEQ AADLIDRCAA ARELGHAADT ISIGGGFGVD
YVPEGAWREF TDGVDRAWFH AGKSFGSYYP YHFPAPGPAM LSAILAYGDL ADRLRDNDIR
LAVEPGRALL DRAGSTVFRV QGSKIRHADG QPYQLLTVDG TSLSLSEQWF DSEYLPDPVL
WPQRPGEPTP TSVGAASCLE SDMLSWRRIP LRRRAEEGDL LVYPNTAGYQ MDSNESAFHE
LPIPPKVVLS DVREDRLRWT LDAG
//
