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Database: UniProt
Entry: Q8FT70_COREF
LinkDB: Q8FT70_COREF
Original site: Q8FT70_COREF 
ID   Q8FT70_COREF            Unreviewed;       373 AA.
AC   Q8FT70; C8NP10;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   SubName: Full=Putative ornithine cyclodecarboxylase {ECO:0000313|EMBL:BAC18510.1};
DE            EC=4.3.1.12 {ECO:0000313|EMBL:BAC18510.1};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18510.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC18510.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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DR   EMBL; BA000035; BAC18510.1; -; Genomic_DNA.
DR   RefSeq; WP_006767701.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FT70; -.
DR   STRING; 196164.gene:10742121; -.
DR   KEGG; cef:CE1700; -.
DR   eggNOG; COG2423; Bacteria.
DR   HOGENOM; CLU_042088_3_4_11; -.
DR   OrthoDB; 9801817at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0008473; F:ornithine cyclodeaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_N.
DR   PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR   PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR   Pfam; PF02423; OCD_Mu_crystall; 1.
DR   PIRSF; PIRSF001439; CryM; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:BAC18510.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001409}.
SQ   SEQUENCE   373 AA;  39917 MW;  93E1C78B1B0A6525 CRC64;
     MINFLFLNET DMIDAGVADI ASCVDVMEET LVLLAQGDYR MAGQNANSHG AMITFPANPA
     FDSMPADGPD RRFMAMPAYL GGRFNNTGVK WYGSNAANRT RGLPRSIHTF VLNDTDTGAP
     KAIMSANLLS AYRTGAVPGV GVKHLAVEHA STLAVIGPGV MARTITEACM ALRSGITTIT
     VKGRSAGGVA AFTDWVHARW PHVTVTAAPT VEKAVDGADI VIAATTTDAA GSSAFPYLRR
     DWLAPGALLL LPAAARFDDS FLTGDARLVV DYMGLYDAWA EEYGDRAYQL LGIPGTHWHD
     LIRAGKLDQG RVRQMGDICE GIMPARLNNE EIILYSVGGM PVEDVAWATQ VYENALIKGI
     GTTVNLWDKP ALV
//
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