(data stored in SCRATCH zone)

SWISSPROT: Q13EP9_RHOPS

ID   Q13EP9_RHOPS            Unreviewed;       448 AA.
AC   Q13EP9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   SubName: Full=FolC bifunctional protein {ECO:0000313|EMBL:ABE37440.1};
DE            EC=6.3.2.17 {ECO:0000313|EMBL:ABE37440.1};
GN   OrderedLocusNames=RPD_0200 {ECO:0000313|EMBL:ABE37440.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37440.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37440.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37440.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001563}.
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DR   EMBL; CP000283; ABE37440.1; -; Genomic_DNA.
DR   RefSeq; WP_011500632.1; NC_007958.1.
DR   STRING; 316057.RPD_0200; -.
DR   EnsemblBacteria; ABE37440; ABE37440; RPD_0200.
DR   KEGG; rpd:RPD_0200; -.
DR   eggNOG; ENOG4105DPM; Bacteria.
DR   eggNOG; COG0285; LUCA.
DR   HOGENOM; HOG000019981; -.
DR   KO; K11754; -.
DR   OMA; YFEMGTL; -.
DR   OrthoDB; 1232874at2; -.
DR   BioCyc; RPAL316057:RPD_RS01015-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   PANTHER; PTHR11136; PTHR11136; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01499; folC; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EP9.
DR   SWISS-2DPAGE; Q13EP9.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:ABE37440.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT   DOMAIN       55    275       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
SQ   SEQUENCE   448 AA;  47901 MW;  7B4AC89440C77C80 CRC64;
     MSAATAPQPS ALVGELRARL AQLHPAQIDL TLGRIERLLA ALDHPQRRLP PVIHIAGTNG
     KGSTLAFLRA ILEAAGLSVH AYTSPHLVRV NETVRLGRPG GGALVSDDEF AAALAHCERV
     NQGAPITLFE IETAAALWLF AQHPADVTLL EVGLGGRLDA TNVIDQPLAC VLTPIGIDHT
     EFLGPTLADI AAEKAGIIRR GVPVIVAGQQ NDAMDVIERE AERLRAPLHA RGQQWHVEVE
     HGRLAYQDDR GLMDLTAPKL FGRHQIDNAW LAIATLRAQQ RFTFDQAAYQ AGLLSADWPA
     RMQRLTTGRL IDEAPPGSEL WLDGGHNADG GRVAAAALGD LEERVSRPLV IIAGMMANKD
     ASAFLTNFTG LTRHVIAVPI PDRDGAMPPE KLADAGRALG LRVELADSVE AALSRIAGLA
     YELPPRILIT GSLYLAGHVL RLNGTMPS
//

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