ID Q2NQ25_SODGM Unreviewed; 401 AA.
AC Q2NQ25;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Achromobactin biosynthetic and transport gene lysA {ECO:0000313|EMBL:BAE75750.1};
DE SubName: Full=L-glutamyl-[BtrI acyl-carrier protein] decarboxylase {ECO:0000313|EMBL:CRL46869.1};
GN Name=btrK {ECO:0000313|EMBL:CRL46869.1};
GN OrderedLocusNames=SGP1_0043 {ECO:0000313|EMBL:BAE75750.1};
GN ORFNames=SGGMMB4_05835 {ECO:0000313|EMBL:CRL46869.1};
OS Sodalis glossinidius (strain morsitans).
OG Plasmid pSG1 {ECO:0000313|EMBL:BAE75750.1,
OG ECO:0000313|Proteomes:UP000001932}, and
OG Plasmid psg1 {ECO:0000313|Proteomes:UP000245838}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE75750.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE75750.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Morsitans {ECO:0000313|EMBL:BAE75750.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000001932};
RC PLASMID=pSG1 {ECO:0000313|EMBL:BAE75750.1,
RC ECO:0000313|Proteomes:UP000001932};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
RN [2] {ECO:0000313|Proteomes:UP000245838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans {ECO:0000313|Proteomes:UP000245838};
RC PLASMID=psg1 {ECO:0000313|Proteomes:UP000245838};
RA Goodhead I.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CRL46869.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B4 {ECO:0000313|EMBL:CRL46869.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; AP008233; BAE75750.1; -; Genomic_DNA.
DR EMBL; LN854558; CRL46869.1; -; Genomic_DNA.
DR RefSeq; WP_011279192.1; NZ_LN854558.1.
DR KEGG; sgl:SGP1_0043; -.
DR HOGENOM; CLU_026444_0_3_6; -.
DR OrthoDB; 9802147at2; -.
DR BioCyc; SGLO343509:SGP1_RS22470-MONOMER; -.
DR Proteomes; UP000001932; Plasmid pSG1.
DR Proteomes; UP000245838; Plasmid psg1.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR CDD; cd06843; PLPDE_III_PvsE_like; 1.
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; IPR002433; Orn_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 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:BAE75750.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 31..279
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 280..371
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 344
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 55
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 401 AA; 44338 MW; FF1057819C4A23FC CRC64;
MTELPVRVVA AIAQARQQQD DPLAMFIYDL AALQQHIRQV MEALPDGAEL YYAIKANSEP
QILQTLAPWV DGFEISSGGE IERLQAAGSD KPFVFSGPGK LDSDLRAALR RQAAAIHVES
LNEIDRLQRL AREQGRVQTV LIRINPQLPA QISSRLAMAG TATPFGIDEA DLAVAVHRVD
NADHLVLQGF HVHAMSHQQS EQRHRQLMEY YLQRWPQWKA LSAQQEGITH LNVGGGIGVD
YLSTSQFDWP GFCHWLGELL AVTAGAPRLR FEPGRFISAF CGYYAIEILD QKTSHGKHFL
VCRGGTHQFR LPVAQGHDHP IIHLPQRSDG AGELCAWTVV GQLCTPKDVL SRDCSLKGVA
IGDMLVLPLA GAYGYNISHA DFLCHPRPCQ LFLPLETASW A
//
