ID A0A1S6ISD5_9FIRM Unreviewed; 421 AA.
AC A0A1S6ISD5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:AQS57679.1};
GN ORFNames=B0537_00170 {ECO:0000313|EMBL:AQS57679.1};
OS Desulforamulus ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS57679.1, ECO:0000313|Proteomes:UP000189464};
RN [1] {ECO:0000313|EMBL:AQS57679.1, ECO:0000313|Proteomes:UP000189464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSS09 {ECO:0000313|EMBL:AQS57679.1,
RC ECO:0000313|Proteomes:UP000189464};
RX PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT compost.";
RL Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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; CP019698; AQS57679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6ISD5; -.
DR STRING; 1833852.B0537_00170; -.
DR KEGG; dfg:B0537_00170; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000189464; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR CDD; cd06828; PLPDE_III_DapDC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR002986; DAP_deCOOHase_LysA.
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; PR01181; DAPDCRBXLASE.
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:UP000189464}.
FT DOMAIN 30..276
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 279..367
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 421 AA; 47184 MW; A844EC7A17F04F00 CRC64;
MKKPFVTLEK LQEIIKQYPT PFHLYDEKGI RENARRLQQA FSWNKGFKEY FAVKATPNPA
ILDILRQEGC GADCSSFTEL MLAQAVGFTG DEIMFSSNVT PREDFAYAHK LNAIINFDDI
THIDFFSQIA PMPETVSLRY NPGGQFKISN AIMDNPGEAK YGLTRAQLTE GIKKLQGMGV
KHFGLHAFLA SNTKTNDYYP ELAKILFTTA VELQRETGAH FAFINLSGGV GIPYHPEEQP
VDIFAIGEGV RRAYEEILTP AGMGDVAIYT ELGRYMLGPY GCLVATVLHE KHIHKDYIGL
DACAANLMRP AMYGAYHHIT VMGKEDLPCD HKYDVTGGLC ENNDKFAIDR MLPKIDIGDL
LVIHDTGAHG FAMGYNYNGK LRSAEILLKE DGSFELIRRA ETPADYFATL NHTDYFKKCL
F
//
