(data stored in SCRATCH zone)

SWISSPROT: D4YWY1_SPHJU

ID   D4YWY1_SPHJU            Unreviewed;       616 AA.
AC   D4YWY1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000256|HAMAP-Rule:MF_00129};
GN   Name=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129,
GN   ECO:0000313|EMBL:BAI94863.1};
GN   OrderedLocusNames=SJA_C1-00290 {ECO:0000313|EMBL:BAI94863.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94863.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94863.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34)
CC       of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000256|HAMAP-
CC       Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00129, ECO:0000256|SAAS:SAAS00693050};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00129, ECO:0000256|SAAS:SAAS00693047}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00129}.
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DR   EMBL; AP010803; BAI94863.1; -; Genomic_DNA.
DR   RefSeq; WP_013038709.1; NC_014006.1.
DR   ProteinModelPortal; D4YWY1; -.
DR   STRING; 452662.SJA_C1-00290; -.
DR   EnsemblBacteria; BAI94863; BAI94863; SJA_C1-00290.
DR   GeneID; 29271739; -.
DR   KEGG; sjp:SJA_C1-00290; -.
DR   eggNOG; ENOG4107RE5; Bacteria.
DR   eggNOG; COG0445; LUCA.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; POG091H01O0; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR026904; GidA-assoc_3.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF7; PTHR11806:SF7; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_assoc; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YWY1.
DR   SWISS-2DPAGE; D4YWY1.
KW   Cell cycle {ECO:0000313|EMBL:BAI94863.1};
KW   Cell division {ECO:0000313|EMBL:BAI94863.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00129, ECO:0000256|SAAS:SAAS00693048};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00129,
KW   ECO:0000256|SAAS:SAAS00693049};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00129};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00129}.
FT   DOMAIN      398    608       GIDA_assoc. {ECO:0000259|Pfam:PF13932}.
FT   NP_BIND      11     16       FAD. {ECO:0000256|HAMAP-Rule:MF_00129}.
FT   NP_BIND     270    284       NAD. {ECO:0000256|HAMAP-Rule:MF_00129}.
SQ   SEQUENCE   616 AA;  66025 MW;  F367A88869DE4658 CRC64;
     MRTSYDVIVV GGGHAGCEAA GAAARKGAAV TLLTFERATV GAMSCNPAIG GLGKGHLVRE
     VDALDGLIAR AADAAAIHYR MLNSSKGAAV QGPRVQADRK RYRAEIHRLL DAQSGLEIVE
     GEAVGLLLAE GAVAGLSLAD GRRLHAPSVV LATGTFLGGK LFRGEETLTG GRISERAATA
     LGVQLRALDL PMGRLKTGTP PRIDGRTIDW AALEAQPSDA EGWTMSALSP GRPLPQLSCA
     ITRTNDRTHA IIREGLGRSP LFSGAIEGRG PRYCPSIEDK VIRFGDRDGH QIFLEPEGLD
     DHLVYPNGIS TSLPADVQLA MVRSMAGLEK ADIRVPGYAV EYDHIDPRAL DATLEVQAIP
     GLFCAGQING TTGYEEAAAQ GLLAGINAAA RARGEGPLIL DRASSYIGVM IDDLVLQGVT
     EPYRMLTARA EYRLRLRADN AGTRLAEIGF EHGVLGEERA AYYARRHDER AAVEEELSRT
     FSATEMARSG APVRQDGARR SLFEWARFPE VGRSLLCELA PTLSRISHDL REELLEDAHY
     APYLERQEAE IAEMRRNERV VIPAGFDFAA IGGLSTEMVE RLTLARPDTL AAAGRIRGIT
     PAALAALLVH IRRRAA
//

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