ID L7VJH6_9FLAO Unreviewed; 608 AA.
AC L7VJH6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=ASNER_087 {ECO:0000313|EMBL:AGC66857.1};
OS Candidatus Uzinura diaspidicola str. ASNER.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Candidatus Uzinura.
OX NCBI_TaxID=1133592 {ECO:0000313|EMBL:AGC66857.1, ECO:0000313|Proteomes:UP000011174};
RN [1] {ECO:0000313|EMBL:AGC66857.1, ECO:0000313|Proteomes:UP000011174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASNER {ECO:0000313|EMBL:AGC66857.1,
RC ECO:0000313|Proteomes:UP000011174};
RX PubMed=23279075; DOI=10.1111/1462-2920.12058;
RA Sabree Z.L., Huang C.Y., Okusu A., Moran N.A., Normark B.B.;
RT "The nutrient supplying capabilities of Uzinura, an endosymbiont of
RT armoured scale insects.";
RL Environ. Microbiol. 15:1988-1999(2013).
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; CP003263; AGC66857.1; -; Genomic_DNA.
DR AlphaFoldDB; L7VJH6; -.
DR STRING; 1133592.ASNER_087; -.
DR KEGG; udi:ASNER_087; -.
DR PATRIC; fig|1133592.3.peg.77; -.
DR HOGENOM; CLU_007831_2_2_10; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000011174; 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.
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:UP000011174};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 533..604
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 608 AA; 68550 MW; A184BDBFC675D81B CRC64;
MMFYDVIVVG GGHAGAEAAA ASARMGSSVL LITMNLHTIG EMSCNPSIGG IATGQIVREI
DALGGFSGII ADHTMIQFRM LNRSKGPAMW SPRAQLDRLR FSDNWRMVLE SIPNISFCQD
SVVELLILNE KVYGVKTMLG VEIKSKAVIL TNGTFLNGFI HIGEKKISGG RISEKSTTGL
SSQLKSLGFD VGRMKTGTSP RVDGRSLNYS EMVEQPGDDY PKKFSYLDTP PLVNQYSCYI
TYTSEKVHEI LRSGFDRSPN FNGSINSKGP RYCPSIEDKI YRFSDRARHQ IFAEPEGLNT
TEVYVNGFST SLPQEFQFDA LHQIPGFEQA KILKPGYAIE YDYFSPLQLN HSLETKKIKN
LFFSGQINGT TGYEVAAAQG LIAGINAHLK IHGKAPFVLL RNEAYIGVLI DDLVTKGTDE
PYRMFTARAE YRILLRQDNA DERLTPSAID LGLVENNRLK KLEEKLNKVE KCVSYLNREI
RTLNKITQPT RIATLLSRPE ISYEDLFFLP EIKEYGKYNK LKEEEWQQVS ILIKYKAYIE
REREMAINLI RLEKIRLPKF FDYKKIQALS VEAQEKLNTH FPSSIGQASR ISGISPSDIN
TLLIYMKR
//
