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
//