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Database: UniProt
Entry: Q32C34_SHIDS
LinkDB: Q32C34_SHIDS
Original site: Q32C34_SHIDS 
ID   Q32C34_SHIDS            Unreviewed;       711 AA.
AC   Q32C34;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=Ornithine decarboxylase isozyme {ECO:0000313|EMBL:ABB63121.1};
GN   Name=speC {ECO:0000313|EMBL:ABB63121.1};
GN   OrderedLocusNames=SDY_3107 {ECO:0000313|EMBL:ABB63121.1};
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB63121.1, ECO:0000313|Proteomes:UP000002716};
RN   [1] {ECO:0000313|EMBL:ABB63121.1, ECO:0000313|Proteomes:UP000002716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197 {ECO:0000313|EMBL:ABB63121.1,
RC   ECO:0000313|Proteomes:UP000002716};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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DR   EMBL; CP000034; ABB63121.1; -; Genomic_DNA.
DR   RefSeq; WP_000839556.1; NC_007606.1.
DR   RefSeq; YP_404612.1; NC_007606.1.
DR   AlphaFoldDB; Q32C34; -.
DR   STRING; 300267.SDY_3107; -.
DR   EnsemblBacteria; ABB63121; ABB63121; SDY_3107.
DR   KEGG; sdy:SDY_3107; -.
DR   PATRIC; fig|300267.13.peg.3716; -.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   OMA; MKGRSGE; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.220; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR005308; OKR_de-COase_N.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR027464; Ornithine_deCO2ase_N.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229:SF4; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   Pfam; PF03709; OKR_DC_1_N; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002716}.
FT   DOMAIN          5..95
FT                   /note="Orn/Lys/Arg decarboxylase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03709"
FT   DOMAIN          101..543
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          568..697
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
FT   MOD_RES         347
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   711 AA;  79598 MW;  D0543E6D19D4D6BF CRC64;
     MKSMDIAASS ELVSRLSSHR RVVALGDTDF TDVAAVVITA ADSRSGILTL LKRTGFHLPV
     FLYSEHAVEL PAGVTAVING NEQHWLELES AACQYEENLL PPFYDTLTQY VEMGNSTFAC
     PGHQHGAFFK KHPAGRHFYD FFGKNVFRAD MCNADVKLGD LLIHEGSAKD AQKFAAKVFH
     ADKTYFVLNG TSAANKVVTN ALLTRGDLVL FDRNNHKSNH HGALIQAGAT PVYLEASRNP
     FSFIGGIDAH CFNEEYLRQQ IRDVAPEKAD LPRPFRLAII QLGTYDGTVY NARQVIDTIG
     HLCDYILFDS AWVGYEQFIP MMADSSPLLL ELNENDPGIF VTQPVHKQQA GFSQTSQIHK
     KDNHIRGQAR FCPHKRLNNA FMLHASTSPF YPLFVALDVN AKIHEGERGR RLWAECVELG
     IESRKAILAR CKLFRPFIPP VVDGKLWQDY PTSVLASDRR FFSFEPGAKW HGFEGYAADQ
     YFVDPCKLLL TTPGIDAETG EYSDFGVPAT ILAHYLRENG IVPEKCDLNS ILFLLTPAES
     HEKLAQLVAM LAQFEQHIED DSPLAEVLPS VYNKYPVRYR DYTLRQLCQE MHDLYVSFDV
     KDLQKAMFRQ QSFPSVVMTP QDAHSAYIRG DVELVRIRDA EGRIAAEGAL PYPPGVLCVV
     PGEVWGGAVQ RYFLALEEGV NLLPGFSPEL QGVYSETDAD GMKRLYGYVL K
//
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