ID Q2NUI9_SODGM Unreviewed; 330 AA.
AC Q2NUI9;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:BAE74186.1};
DE SubName: Full=D-cysteine desulfhydrase {ECO:0000313|EMBL:CRL44748.1};
GN Name=dcyD {ECO:0000313|EMBL:CRL44748.1};
GN OrderedLocusNames=SG0911 {ECO:0000313|EMBL:BAE74186.1};
GN ORFNames=SGGMMB4_02011 {ECO:0000313|EMBL:CRL44748.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE74186.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE74186.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Morsitans {ECO:0000313|EMBL:BAE74186.1}, and morsitans
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|EMBL:CRL44748.1, ECO:0000313|Proteomes:UP000245838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:CRL44748.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000245838};
RA Goodhead I.;
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 -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000256|ARBA:ARBA00008639}.
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DR EMBL; AP008232; BAE74186.1; -; Genomic_DNA.
DR EMBL; LN854557; CRL44748.1; -; Genomic_DNA.
DR RefSeq; WP_011410772.1; NZ_LN854557.1.
DR STRING; 343509.SG0911; -.
DR KEGG; sgl:SG0911; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OrthoDB; 9801249at2; -.
DR BioCyc; SGLO343509:SGP1_RS07745-MONOMER; -.
DR Proteomes; UP000001932; Chromosome.
DR Proteomes; UP000245838; Chromosome sggmmb4_Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01275; ACC_deam_rel; 1.
DR PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR006278-2}.
FT DOMAIN 20..313
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 53
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 330 AA; 34888 MW; CA8070FC429E19F9 CRC64;
MSDLAQRLAG VPRLDIIGPP TPLEHLPRLS DFLARDIFIK RDDLTPLGLG GNKLRKLEYL
AADALRQGAD TLLTAGAIQS NHVRQTAALA AKLGLHCVAL LEKPIDTPAG NYLTNGNRLL
LDLFQCEVIA CEALTQPAQQ LADASLRLEA QGFRPYVIPV GGSNALGSLG YVGCALEIAH
QCQGVIQPGA VVVSSGSGGT HAGLEVGLAA VLPETAFIGV TVSRRSEQQR PLIASLAAQV
SEQLSLAAPA AEITLWDEYF APGYGQLNDE GREAIALLAR LEGIVLDPVY AGKAMAGLID
GLERDRFPDG PLVCSCIPAA LFAYHYLETR
//
