ID A0A164CJS9_9SYNE Unreviewed; 658 AA.
AC A0A164CJS9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:KZR90376.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=MITS9508_00926 {ECO:0000313|EMBL:KZR90376.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR90376.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR90376.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR90376.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) 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:KZR90376.1}.
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DR EMBL; LVHU01000003; KZR90376.1; -; Genomic_DNA.
DR RefSeq; WP_067093726.1; NZ_LVHU01000003.1.
DR AlphaFoldDB; A0A164CJS9; -.
DR STRING; 1801629.MITS9508_00926; -.
DR PATRIC; fig|1801629.3.peg.995; -.
DR Proteomes; UP000076799; 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.
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 565..636
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 293..307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 658 AA; 71794 MW; F8A41A3BEE35F1B5 CRC64;
MSSSPDPTEV FDVIVVGGGH AGCEAAITAA RLGLNTALFT LNLDRIAWQP CNPAVGGPAK
SQLVHEVDAL GGVIGRLADA TAIQKRILNA SRGPAVWALR AQTDKRQYSR QMLQLLQHTP
NLALREAMVT GLEIEGDPNG GGKAWNPSQG TAARITGVST YFGSVYGAKA VVLTAGTFLG
GRIWVGHQSM AAGRAGEQAA EGLTEALQQL GFHTDRLKTG TPARVDRRSI ALDQLEEQPS
DAADRFFSFD PGSWSSGEQM SCHITRTTAA THQLIKDNLH LTAIYGGVID SKGPRYCPSI
EDKIVRFADK DSHQIFLEPE GRDTPEIYVQ GFSTGLPEPI QLQLLRSLPG LEQCVMLRPA
YSVDYDYLPA TQLLPSLETK RVEGLFSAGQ LNGTTGYEEA AAQGLVAGLN AVRRIRGQEA
MHFSRESSYI GTMIDDLVSK DLREPYRVLT SRSEYRLVLR GDNADRRLTP LGRDLGLIDD
RRWQLFEQKL AAMEAEKQRL QSKRLKVSDP VAAAVEAETG APIKGSITLA DLLRRPGMHA
ADLVRLGLAD ADLPLPVREG AEIDIKYSGY LQRQQQQIDQ VRRQGKRKLP AGIDYANINT
LSREAREKLT DVRPLTLGQA SQIPGVSQAD LSALLVWLEL QQRRDQKRTT LASSSNAR
//
