ID F7XH45_SINMM Unreviewed; 408 AA.
AC F7XH45;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Decarboxylase {ECO:0000313|EMBL:AEH83871.1};
GN OrderedLocusNames=SM11_pD1039 {ECO:0000313|EMBL:AEH83871.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11d {ECO:0000313|EMBL:AEH83871.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH83871.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH83871.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH83871.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11d {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
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; CP001832; AEH83871.1; -; Genomic_DNA.
DR RefSeq; WP_014530614.1; NZ_JAJJBH010000002.1.
DR AlphaFoldDB; F7XH45; -.
DR KEGG; smx:SM11_pD1039; -.
DR PATRIC; fig|707241.3.peg.6726; -.
DR HOGENOM; CLU_026444_0_3_5; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11d.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
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; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_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 PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Plasmid {ECO:0000313|EMBL:AEH83871.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 44..290
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 291..386
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 66
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 408 AA; 43962 MW; 84F8B2C5DADC3B5A CRC64;
MNSHPTIALY DVVGNWLSVG GIPINRLAEC VGGTPFFAYD RQLITSRVKF LRSVLPSDIH
LSYAVKANPM PAVVQHLARL VDAFDVASTT EMKTALDTPT PASHISFAGP GKTMVELTQA
VAAGVTIEIE SPTEAARVVE VGSRLGIRPR VALRINPDFQ IKGSGMRMGG GPQQFGIDVE
EIPSLLQKLA AAELDFLGFH VFSGSQNLHA DILCEALAKH VSLLIRLAGE CPWPVRYLNL
GGGFGIPYFE KDRPLDLFAI GETLSDLMEC AVRPNLPDAR VVIELGRYLV GESGVYVTRV
VDRKVSRGKV YLVVDGGLHH QLAASGNFGQ VIRRNYPIAV ANRMKETEFE NVSVVGCLCT
PLDMLGDNIT LPRADIGDLL VVFQAGAYGL TASPTAFLGH PLPVEILA
//
