GenomeNet

Database: UniProt
Entry: A0A1Q5PF85_9BACT
LinkDB: A0A1Q5PF85_9BACT
Original site: A0A1Q5PF85_9BACT 
ID   A0A1Q5PF85_9BACT        Unreviewed;       620 AA.
AC   A0A1Q5PF85;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=A3841_13310 {ECO:0000313|EMBL:OKL40821.1};
OS   Pontibacter flavimaris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1797110 {ECO:0000313|EMBL:OKL40821.1, ECO:0000313|Proteomes:UP000186551};
RN   [1] {ECO:0000313|EMBL:OKL40821.1, ECO:0000313|Proteomes:UP000186551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S10-8 {ECO:0000313|EMBL:OKL40821.1,
RC   ECO:0000313|Proteomes:UP000186551};
RA   Zhang G., Zhang R.;
RT   "Genome sequence of Pontibacter sp. nov., of the family cytophagaceae,
RT   isolated from marine sediment of the Yellow Sea, China.";
RL   Submitted (MAR-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:OKL40821.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LVWA01000004; OKL40821.1; -; Genomic_DNA.
DR   RefSeq; WP_073851441.1; NZ_LVWA01000004.1.
DR   AlphaFoldDB; A0A1Q5PF85; -.
DR   STRING; 1797110.A3841_13310; -.
DR   OrthoDB; 9815560at2; -.
DR   Proteomes; UP000186551; 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          545..616
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         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   620 AA;  69006 MW;  7F2AAA705CD552CA CRC64;
     MFPEYDIIVV GAGHAGCEAA AAAAKMGSKV LLATMNMNTI AQMSCNPAMG GVAKGQIVRE
     VDALGGMSGI ITDQTMIQFR MLNKSKGPAM WSPRAQSDRM RFAEAWRLSL EQTENVDFWQ
     EMVTSIEVEN GRAVGVRTSL GITIRGKAVI LTNGTFLNGI IHIGEKQMGG GRSAEKAAKG
     ITEQLKELGF EAGRMKTGTP PRVDGRSLDY SKMEEQFGDE NPSKFSYTDT QPLPKQRSCY
     ITYTNPEVHE ILKTGFEKSP MFQGRIQGLG PRYCPSIEDK INRFADRTRH QIFVEPEGWN
     TVEVYVNGFS SSLPEHVQYE ALRKIEGFEN AKMFRPGYAI EYDFFPPTQL NLTLETKLVQ
     NLYFAGQING TTGYEEAACQ GLMAAINAHN KINDKEPFIL KRSEAYIGVL IDDLVNKGTD
     EPYRMFTSRA EHRILLRQDN ADIRLTKMGY ELGLADESRM QAVDKKITET AEIIAYLNNK
     PIEPGNINSM LEELGSAPIT EKQRAGQLIK RPNVEIEDIA RAIPAVAEYL SKFKPDSVEQ
     AGIQVKYETY IEKEYAMAAK MGELENYTIK GKINYRDIPA LSKEAKEKLL KVEPETIGQA
     SRISGVSPAD ISVLMVYLGK
//
DBGET integrated database retrieval system