(data stored in SCRATCH zone)

SWISSPROT: E6UXS9_VARPE

ID   E6UXS9_VARPE            Unreviewed;       652 AA.
AC   E6UXS9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|HAMAP-Rule:MF_00129, ECO:0000256|SAAS:SAAS01147114};
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   OrderedLocusNames=Varpa_0050 {ECO:0000313|EMBL:ADU34273.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34273.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34273.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34273.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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, ECO:0000256|SAAS:SAAS01147112}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00129, ECO:0000256|SAAS:SAAS01080909};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00129,
CC       ECO:0000256|SAAS:SAAS01147118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129,
CC       ECO:0000256|SAAS:SAAS01147113}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00129, ECO:0000256|SAAS:SAAS01080916}.
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; CP002417; ADU34273.1; -; Genomic_DNA.
DR   RefSeq; WP_013538520.1; NC_014931.1.
DR   STRING; 595537.Varpa_0050; -.
DR   EnsemblBacteria; ADU34273; ADU34273; Varpa_0050.
DR   GeneID; 29714853; -.
DR   KEGG; vpe:Varpa_0050; -.
DR   eggNOG; ENOG4107RE5; Bacteria.
DR   eggNOG; COG0445; LUCA.
DR   HOGENOM; HOG000201060; -.
DR   KO; K03495; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   BioCyc; VPAR595537:G1GQO-50-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR026904; GidA-assoc_3.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF13932; GIDA_assoc; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6UXS9.
DR   SWISS-2DPAGE; E6UXS9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129,
KW   ECO:0000256|SAAS:SAAS01147115};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00129, ECO:0000256|SAAS:SAAS01080904};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00129,
KW   ECO:0000256|SAAS:SAAS01080908};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00129, ECO:0000256|SAAS:SAAS01147117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00129,
KW   ECO:0000256|SAAS:SAAS01147111}.
FT   DOMAIN      408    625       GIDA_assoc. {ECO:0000259|Pfam:PF13932}.
FT   NP_BIND      13     18       FAD. {ECO:0000256|HAMAP-Rule:MF_00129}.
FT   NP_BIND     279    293       NAD. {ECO:0000256|HAMAP-Rule:MF_00129}.
SQ   SEQUENCE   652 AA;  71722 MW;  15300C2A0FE6B434 CRC64;
     MLYPEEFDVI VVGGGHAGTE AALAAARMGA KTLLLSHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AIATDEAGIQ FRILNSSKGP AVRATRAQAD RVLYKAAIRH RLENQPNLSL
     FQQAVDDLMV EGDRVVGAVT QVGIAFRART VVLTAGTFLD GRIHVGLDNY QAGRAGDPPA
     ISLSARLKEL KLPQGRLKTG TPPRLDGRSI DFSKCTEQPG DGMPGGAGPM PVFSFMGRAD
     MHPRQMACWI THTNARTHDI IRSGFDRSPM FTGKIDGVGP RYCPSVEDKI NRFADKESHQ
     IFLEPEGLTT NEYYPNGIST SLPFDIQYQL VRSMPGLENA HILRPGYAIE YDYFDPRELK
     SSFETRSVKG LFFAGQINGT TGYEEAAAQG LFAGINAALQ CRGEDAWLPR RDEAYLGVLV
     DDLITKGVTE PYRMFTSRAE FRLQLREDNA DMRLTEAGRK LGLVDDARWD AFSRKRDAVS
     RETERLKSIW VNPRNLPAAE SERVLGKAIE HEYNLADLLR RPDVNYETLM SLDGGKYSAS
     SALSETEIEQ IEISAKYSGY IERQHDEVER AAHFENLRLP ADFDYGQVKA LSFEVRQKLD
     KHRPETLGLA SRISGVTPAA ISLLMIHLRK GGHKAFARDA ATEAAAEPQS AE
//

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