ID K0P5M8_9BACT Unreviewed; 620 AA.
AC K0P5M8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:CCM10093.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=CAHE_0316 {ECO:0000313|EMBL:CCM10093.1};
OS Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Cardinium.
OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM10093.1, ECO:0000313|Proteomes:UP000003996};
RN [1] {ECO:0000313|EMBL:CCM10093.1, ECO:0000313|Proteomes:UP000003996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA Malfatti S.A., Hunter M.S., Horn M.;
RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT Incompatibility in Cardinium hertigii.";
RL PLoS Genet. 8:e1003012-e1003012(2012).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00129}.
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DR EMBL; HE983995; CCM10093.1; -; Genomic_DNA.
DR RefSeq; WP_014934467.1; NC_018605.1.
DR AlphaFoldDB; K0P5M8; -.
DR STRING; 1231626.CAHE_0316; -.
DR KEGG; che:CAHE_0316; -.
DR PATRIC; fig|1231626.3.peg.311; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_10; -.
DR OrthoDB; 9815560at2; -.
DR BioCyc; CEND1231626:AL022_RS01430-MONOMER; -.
DR Proteomes; UP000003996; 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; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
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 Pfam; PF21680; GIDA_C_1st; 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 545..616
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 270..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 620 AA; 69248 MW; 9CFE7F2D156C06E6 CRC64;
MVLEYDIIVV GGGHAGCEAA TAAAKLGAKV LLVTMSLQTI GQMSCNPAMG GIAKGQLIRE
IDALGGFSGS IADQSAIQFR MLNTSKGPAM WSPRTQNDRG LFSIYWRRAL ESLPNLDFWQ
DMVVSLLVKN RQVQGIQTAL GISIKGRAVI LTNGTFLNGI IHIGAKKMAG GRSGEKAATG
ITEQLQKLGF QTGRMKTGTS PRVDGRTLDY NKMEKQPGDP VPGTFSFLNT SPLIKQKNCY
ITHTNPTVHN LIKDNLADVP IYNGQIQSTG PRYCPSIEDK VYRFADKERH QIFIEPEGWH
TIQVYVNGLS TSLPEAIQLK MLRAITGFEK VKMICPGYAI EYDYFPPTQL YYTLETQLIQ
NLYFAGQING TTGYEEAASQ GLMAGINAYR KMHELSQIVF KRSEAYIGVL IDDLVGKGTE
EPYRMFTSRA EFRILLRQDN ADLRLTELGY AIGLADEERL QRVYKKKKAL VSIFDFLKKW
KIQPEIINPI LAAQGASLID IPQYADGLLK RPEVDLNDLL QLDKQQSNAL FTYGEEVLQQ
ANIQVKYENY FQKEKELVEK MEQLEHYTIP LDFNYTKLKA ISAEGLEKLQ KVRPATLGQA
SRISGVRPAD ISILMVYLGR
//
