ID A0A429XVS6_9RICK Unreviewed; 595 AA.
AC A0A429XVS6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:RST72464.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=EIC27_00275 {ECO:0000313|EMBL:RST72464.1};
OS Candidatus Aquarickettsia rohweri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Aquarickettsia.
OX NCBI_TaxID=2602574 {ECO:0000313|EMBL:RST72464.1, ECO:0000313|Proteomes:UP000279470};
RN [1] {ECO:0000313|Proteomes:UP000279470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a_cerv_44 {ECO:0000313|Proteomes:UP000279470};
RA Klinges J.G., Rosales S.M., Mcminds R., Shaver E.C., Shantz A.,
RA Peters E.C., Burkepile D.E., Silliman B.R., Vega Thurber R.L.;
RT "Phylogenetic, genomic, and biogeographic characterization of a novel and
RT ubiquitous marine invertebrate-associated Rickettsiales parasite,
RT Candidatus Marinoinvertebrata rohwerii, gen. nov., sp. nov.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RST72464.1}.
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DR EMBL; RXFM01000002; RST72464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429XVS6; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000279470; 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:UP000279470};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 516..587
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 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 595 AA; 67394 MW; A976F099F455E651 CRC64;
MKKDYDVIII GGGHAGIEAA AASCRIGAKT CLITKSKNDL GQLSCNPSIG GVAKGIIVRE
IDALDGIMSK AIDRSGIHFK MLNRSKGPAV WGLRAQADRD LFKLNIEKII ENYPNLNILY
NTVDDIIIDN NKVIGVICDK VKIYSNSVVI TSGTFLNGKI YIGEQNYSGG RYGEKSITTL
AKKLKDYKFK VGRLKTGTPP RINKNSINWK ILEEQLGDTN PYLFSDLSQN TLQKQISCYI
TYTNKKTHQI LLDNLHKSAI YSGKISSNGP RYCPSIEDKI MRFKDKERHQ IFLEPEGLES
DLVYPNGIST SLPKNVQEKF VRSIYGLENA KITRWGYAIE YDFIDPRELK ETLETKKISN
LFFAGQINGT TGYEEAAGQG VIAGANAALK LNSKQLILSR SDSYIGVMIN DLTNFGTEEP
YRMMTSRAEY RIKLRNDNAT ERLTEIGKKY GLISAKKLKN YQDICTEKNK TEDLIKSKQF
IWNFKNTDDY IHQIKSYFSE IAKTDNRILI KIYAENLYKN YEKRLLKDIE ILKKDKEVII
PKILNFDEIK GLSNEIRTKL KNTSPQTIAD IKRIQGMMPS ALIAIIIYLK KPQDV
//
