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Database: UniProt
Entry: C6HVS6_9BACT
LinkDB: C6HVS6_9BACT
Original site: C6HVS6_9BACT 
ID   C6HVS6_9BACT            Unreviewed;       613 AA.
AC   C6HVS6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   13-SEP-2023, entry version 48.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461, ECO:0000256|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800, 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   ORFNames=UBAL3_79520022 {ECO:0000313|EMBL:EES53300.1};
OS   Leptospirillum ferrodiazotrophum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=412449 {ECO:0000313|EMBL:EES53300.1, ECO:0000313|Proteomes:UP000009374};
RN   [1] {ECO:0000313|EMBL:EES53300.1, ECO:0000313|Proteomes:UP000009374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA   Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA   Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA   Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT   "Community genomic and proteomic analyses of chemoautotrophic iron-
RT   oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT   ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL   Appl. Environ. Microbiol. 75:4599-4615(2009).
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC       certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
CC       {ECO:0000256|ARBA:ARBA00003717, ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_00129};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000256|ARBA:ARBA00025948, 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|ARBA:ARBA00007653,
CC       ECO:0000256|HAMAP-Rule:MF_00129}.
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DR   EMBL; GG693865; EES53300.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HVS6; -.
DR   Proteomes; UP000009374; Unassembled WGS sequence.
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; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR047001; MnmG_C_subdom.
DR   InterPro; IPR044920; MnmG_C_subdom_sf.
DR   InterPro; IPR040131; MnmG_N.
DR   NCBIfam; TIGR00136; gidA; 1.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SMART; SM01228; GIDA_assoc_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00129};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00129};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00129};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009374};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          535..603
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         16..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         183
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         281..295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   613 AA;  67898 MW;  BC43BFE48A80287C CRC64;
     MTQHREKNHW DVVVVGGGHA GIEAAYASAR QGSRTLLLTL HLDFIGQMSC NPSVGGIGKG
     HIVREIDAMG GAMGSLADQS ALQLRVLNTR KGAAVQAIRA QCDRHRYRTL ARRLLDSHPL
     LFLRQGEVVS LERSGDRLSS LALSDGSRIF FDALVLTSGT FLNGQLHIGL SSTSGGRGGE
     RSSLSLSQFL SEECGLSLGR LKTGTPPRLH GRSLDFSRME PQPGDEPLPF FSQLSPPPEG
     LFFGGSSLPC YLTHTTPETR DIIQKNLDRS PLYSGKIRGI GPRYCPSIED KIVKFPDHLT
     HHIFIEPEGL DVDEFYPNGI STSLPVDVQE QILSSIPGLE NAIILRPGYA VEYDFVFPDQ
     LHHTLAVKST PNLFLAGQIN GTTGYEEAAG QGLVAGINAA RHSQGLSTWT PDRQSSYIGV
     MVDDLVTHSI DEPYRMFTSR AENRLYIRND NAVERMTPQA LALGLLSPQQ IEAFNDRIEY
     QNSLRALLHS SRLEGKSLHH RLRSPDVTLR QLLREQAIDF SAIPPLWLDA LEQEIKYEGY
     VRISMDRWDR MADLPIPPSF FDRDIPGLSN EVRTRLRKSR PTTLHQALSL RGMTPGAIDL
     LRIYLTKELP PSA
//
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