(data stored in ACNUC7421 zone)

SWISSPROT: C8W518_DESAS

ID   C8W518_DESAS            Unreviewed;       688 AA.
AC   C8W518;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   SubName: Full=Cytidyltransferase-related domain protein {ECO:0000313|EMBL:ACV61370.1};
DE            EC=6.2.1.22 {ECO:0000313|EMBL:ACV61370.1};
GN   OrderedLocusNames=Dtox_0439 {ECO:0000313|EMBL:ACV61370.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61370.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61370.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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DR   EMBL; CP001720; ACV61370.1; -; Genomic_DNA.
DR   RefSeq; WP_015756091.1; NC_013216.1.
DR   STRING; 485916.Dtox_0439; -.
DR   EnsemblBacteria; ACV61370; ACV61370; Dtox_0439.
DR   KEGG; dae:Dtox_0439; -.
DR   eggNOG; ENOG4105DUA; Bacteria.
DR   eggNOG; COG3053; LUCA.
DR   OrthoDB; 1354563at2; -.
DR   BioCyc; DACE485916:G1GFV-450-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR005216; Citrate_lyase_ligase.
DR   InterPro; IPR013166; Citrate_lyase_ligase_C.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR40599; PTHR40599; 1.
DR   Pfam; PF08218; Citrate_ly_lig; 1.
DR   SMART; SM00764; Citrate_ly_lig; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   4: Predicted;
DR   PRODOM; C8W518.
DR   SWISS-2DPAGE; C8W518.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Ligase {ECO:0000313|EMBL:ACV61370.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000313|EMBL:ACV61370.1}.
FT   DOMAIN      495    676       Citrate_ly_lig. {ECO:0000259|SMART:
FT                                SM00764}.
SQ   SEQUENCE   688 AA;  80428 MW;  B3030BA2CA050E83 CRC64;
     MNHFYYYELC EILSFVAAGK LAVLNSIEEE SENYIQFFRK NHIDVINNEN NQIQEKDLFF
     IYTIYSENGV NKIIDSGCEF ILPIMEYSGQ LPMQSLKERV AKLQGHFQNR TGKLILLSDQ
     KTCDLFEELN FIPDFFINTS GFIESNTERV NPKPGVPRNA FFLIYTSVEL GQLFEKLKYY
     QAFYFANDEK VHLPTVYLIN KIGKLKRDKN VKVYYFNPPV LAAVKHPSEN EKMIMDAFSK
     CTLYEFIGML IEGKFHDSLV NHKLEYFTKD YMKEILHIPR LIQINQLKSL EDYESQYVNI
     KGGKRFTTDA PDQYKNIIHC FGSSQTYSFG VEDKYTFSSC LQRRVNKNYP DTYLVLNYGV
     VGYFACHMLK AMDNAQINEG DIIIFYTAID SEYFFDFAVA ADITTYNFQP MFQRPHNMGD
     VFIDTTHINH YGLEKLTEKA FKVMFTYKDI LNDFSEIRTS KLNEPLNQIT SNPEFANYLS
     YLAEEKIVDF NQKKIGSVVM NCNPFTLGHQ YLIQFASESV DYLYIFLVEE DRSVFSFEDR
     YNMVKAGISK FDNVKLLRSG NFIISSITFP EYFTKETNKD VIIDPSLDLD IFGNCIAKAL
     NISVRFAGEE PFDPITKQYN RFMENLLKKY DIKFVEIKRK EYLDSPISAS RVRKLLKEGN
     LEEMKKIVPK TTYDYLLNCW KGLDSCHR
//

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