ID B2IYA9_NOSP7 Unreviewed; 670 AA.
AC B2IYA9;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=Npun_R6439 {ECO:0000313|EMBL:ACC84708.1};
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC84708.1, ECO:0000313|Proteomes:UP000001191};
RN [1] {ECO:0000313|Proteomes:UP000001191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACC84708.1, ECO:0000313|Proteomes:UP000001191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX PubMed=23463784; DOI=10.1104/pp.112.213116;
RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT Cyanobacterium-Plant Symbiosis.";
RL Plant Physiol. 161:1984-1992(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}.
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; CP001037; ACC84708.1; -; Genomic_DNA.
DR AlphaFoldDB; B2IYA9; -.
DR STRING; 63737.Npun_R6439; -.
DR EnsemblBacteria; ACC84708; ACC84708; Npun_R6439.
DR KEGG; npu:Npun_R6439; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_3; -.
DR PhylomeDB; B2IYA9; -.
DR Proteomes; UP000001191; 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 Reference proteome {ECO:0000313|Proteomes:UP000001191};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 582..653
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 49..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 310..324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 670 AA; 74840 MW; 718F3167F50C086E CRC64;
MITFLLESYI HETTGTAKIE KNSKLADPVS MTMHNSVEFQ DAFDVIVVGA GHSGCEAALA
SARLGCRTLL LTLNLDRIAW QPCNPAVGGP AKSQLTHEVD ALGGEIGKVA DRTYLQKRIL
NSSRGPAVWA LRAQTDKREY AAVMKNIVEN QENLTIRESM VTDLVLGAND EVIGVETYFG
VGFRCKAVIL TTGTFLGGKI WVGNKSMPAG RAGEFAAEGL TQTLNRLGFE TGRLKTGTPA
RVDKRSVDYS KMLIQPGDED VRWFSFDPEA WVEREQMPCY ITRTTTETHR LIQDNLHLSP
VYGGWVEAKG PRYCPSIEDK IVRFADKESH QIFIEPEGRD IPELYIQGFS TGLPENLQLQ
MLRTLPGLEK CVMLRPAYAV EYDYLPATQC YPTLMTKKVA GLFCAGQING TTGYEEAAAQ
GLVAGINAAR FVHSQEMIVF AREQSYIGTL VDDLCTKDLR EPYRMLTSRS EYRLLLRSDN
ADQRLTTLGR EIGLIDDRRW DLFTQKQANI ITEKQRLQAT RVKEHDEMGI AIASDTQQAI
KGSITLNDLL RRPGFHYVDL DRFGLGNPNL NRAEKEGAEI DIKYYGYLAR QQNQIDQIAR
QAHRQLPADL DYTTIDTLSK EAREKLTHVK PLTLGQAARI GGVNPADVNA LLLYLELRKI
NSQQEFPALA
//
