ID   A0A1I2MTE9_9GAMM        Unreviewed;       411 AA.
AC   A0A1I2MTE9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SFF94752.1};
GN   ORFNames=SAMN05216175_10281 {ECO:0000313|EMBL:SFF94752.1};
OS   Neptunomonas qingdaonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptunomonas.
OX   NCBI_TaxID=1045558 {ECO:0000313|EMBL:SFF94752.1, ECO:0000313|Proteomes:UP000198623};
RN   [1] {ECO:0000313|Proteomes:UP000198623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10971 {ECO:0000313|Proteomes:UP000198623};
RA   Varghese N., Submissions S.;
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}.
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DR   EMBL; FOOU01000002; SFF94752.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2MTE9; -.
DR   STRING; 1045558.SAMN05216175_10281; -.
DR   Proteomes; UP000198623; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   CDD; cd06839; PLPDE_III_Btrk_like; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR017530; DCO2ase_PEP1.
DR   InterPro; IPR022643; De-COase2_C.
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   NCBIfam; TIGR03099; dCO2ase_PEP1; 1.
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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          40..389
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   DOMAIN          49..294
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   ACT_SITE        362
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   411 AA;  44747 MW;  2939D13B60603E38 CRC64;
     MKKEAPKHAH MDWFPVIDNC LHAGGQSITR LAARVGQTPF YVYDRNIMTR KVELLREALP
     QGLHLHYAMK ANPMPAVVQH LSQLTNGIDV ASVAEMQVAL NTGIDPLTIS FAGPGKNDAE
     LRSAIAAGII INMESEGEME RIAQIGESLE ILPHVAIRVN PDFELKTSGM KMGGGPKPFG
     VDAERVPEML KRCGELNLNF KGFHIFSGSQ NLRPEAIIEA QTKTFALAYR LAEFAPQPIT
     WLNIGGGLGI PYFPGEETLP LDAIADNLKP LIIEAQARLP DAEIVMELGR YFVGEAGLYI
     SEVVECKESR GEKFAITNGG LHHHLSASGN FGQIIRKNYP VCVANNVSSD SLEKVSVVGP
     LCTPLDIITD KMLLPVVVIG DLIAVYQSGA YGFTASPRDF LSHPHPLEIL V
//