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Database: UniProt
Entry: A0A0X8FB81_9LACT
LinkDB: A0A0X8FB81_9LACT
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ID   A0A0X8FB81_9LACT        Unreviewed;       634 AA.
AC   A0A0X8FB81;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=AWM72_04200 {ECO:0000313|EMBL:AMB94018.1}, CYJ28_09200
GN   {ECO:0000313|EMBL:PKZ20787.1};
OS   Aerococcus sanguinicola.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX   NCBI_TaxID=119206 {ECO:0000313|EMBL:AMB94018.1, ECO:0000313|Proteomes:UP000069912};
RN   [1] {ECO:0000313|EMBL:AMB94018.1, ECO:0000313|Proteomes:UP000069912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG43001 {ECO:0000313|EMBL:AMB94018.1,
RC   ECO:0000313|Proteomes:UP000069912};
RX   PubMed=27103727;
RA   Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA   Christensen J.J.;
RT   "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT   Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT   Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT   and Aerococcus viridans CCUG 4311T.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000069912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG43001 {ECO:0000313|Proteomes:UP000069912};
RA   Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA   Christensen J.J.;
RT   "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT   Illumina Hiseq.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PKZ20787.1, ECO:0000313|Proteomes:UP000234239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMB0139 {ECO:0000313|EMBL:PKZ20787.1,
RC   ECO:0000313|Proteomes:UP000234239};
RA   Thomas-White K., Wolfe A.J.;
RT   "Phylogenetic diversity of female urinary microbiome.";
RL   Submitted (DEC-2017) 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}.
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DR   EMBL; CP014160; AMB94018.1; -; Genomic_DNA.
DR   EMBL; PKGY01000006; PKZ20787.1; -; Genomic_DNA.
DR   RefSeq; WP_067973693.1; NZ_PKGY01000006.1.
DR   AlphaFoldDB; A0A0X8FB81; -.
DR   GeneID; 69593923; -.
DR   KEGG; asan:AWM72_04200; -.
DR   OrthoDB; 9815560at2; -.
DR   Proteomes; UP000069912; Chromosome.
DR   Proteomes; UP000234239; 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   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:UP000069912};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          552..623
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         280..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   634 AA;  70459 MW;  60AE0508D8F1F29D CRC64;
     MVEQFAAGDY DVIVVGAGHA GCEAALATSR MGQKTLLITI SIDMVAFMPC NPSIGGPAKG
     VVVREIDALG GEMGVNIDKT YIQMRMLNVG KGPAVRALRA QADKEAYART MRQTVEAQEN
     LDLRQGIVSD LVVEEGQCRG VITETGAVFR SQAVILTVGT AARGEIIIGD LKYSSGPNNS
     QAATELTKNL AEKYGFDIVR FKTGTPPRVA KDSVDYDQTS IQPGDETPHH FSFLSDDEDY
     LPADEQIPCW LTYTNEGTHE IIRENLDRAP MFTGIVDGVG ARYCPSIEDK IVRFADKDKH
     QLFLEPEGRY TNEIYVQGLS TSMPEEVQEA MIHSIKGLEK ARIMRDGYAI EYDVVRPNQL
     KMTFETKHID NLYTAGQTNG TSGYEEAAGQ GLYAGINAAL KIQGKDPFII GRDEAYIGVM
     VDDLVTKGTT EPYRLLTSRA EYRLLLRHDN ADLRLTEYGR QLGLVTDERY QRYLFEQNAV
     MSELNRLQTT RLKPTAELQA YLEDKGSSRL KDGILAADLL KRPELKITDI LKFAPSDTDY
     PHEVWDQVEI QVKYAGYIEK AQRNVDKLHR MESKVIPEDI DWDAIEGIAT EARQRLAEIG
     PRTLAQASRV SGVNPADISI LAVYLQSGKV KRRV
//
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