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Database: UniProt
Entry: A0A1Z1FE45_9SPHN
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ID   A0A1Z1FE45_9SPHN        Unreviewed;       619 AA.
AC   A0A1Z1FE45;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=A9D14_13590 {ECO:0000313|EMBL:ARU17006.1};
OS   Croceicoccus marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=450378 {ECO:0000313|EMBL:ARU17006.1, ECO:0000313|Proteomes:UP000195807};
RN   [1] {ECO:0000313|EMBL:ARU17006.1, ECO:0000313|Proteomes:UP000195807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4A9 {ECO:0000313|EMBL:ARU17006.1,
RC   ECO:0000313|Proteomes:UP000195807};
RA   Wu Y.-H., Cheng H., Xu L., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT   "Complete genome sequence of esterase-producing bacterium Croceicoccus
RT   marinus E4A9.";
RL   Submitted (JAN-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; CP019602; ARU17006.1; -; Genomic_DNA.
DR   RefSeq; WP_066847437.1; NZ_CP019602.1.
DR   AlphaFoldDB; A0A1Z1FE45; -.
DR   STRING; 450378.GCA_001661675_02729; -.
DR   KEGG; cman:A9D14_13590; -.
DR   OrthoDB; 9815560at2; -.
DR   Proteomes; UP000195807; 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   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   PRINTS; PR00411; PNDRDTASEI.
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:UP000195807};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          537..608
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         10..15
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   619 AA;  67618 MW;  45509FE69CC8238E CRC64;
     MLQFDVIVVG AGHAGCEAAA AAARMGASVA LVTFDKAKTG AMSCNPAIGG LGKGHLVREV
     DAFDGLIARA ADHAAIHYRM LNRSKGSAVQ GPRVQADRRL FREAIQAMIA KTDNCTEIEG
     EVAALILKGD RVGGVILADG TRLASGAVIL CTGTFLGGRL FRGEERFEGG RIGESGAKRL
     AEQLRAADLP MARLKTGTPP RLDGRSVDWQ SLERQTSDSD QWLMSPLSNG RSNPQLFCAI
     TRTNEQAHDI IRGGLDRSPL FSGAIDSRGP RYCPSIEDKI HRFPDRDGHQ IFLEPEGLDS
     TLIYPNGIST SLPVDIQHGM LRTIEGLEQV RIVEPGYAVE YDHIDPRALT SQLELKAMPG
     LFCAGQINGT TGYEEAAAQG LLAGLHAAAN VLGREGPSLD RANSYLAVMV DDLTPHGVTE
     PYRMLTARAE YRLRLRANNA TTRLTGIGLH IGCIGPERRQ WFERRTEDRT AVESWLDRYF
     HPSVIVSRGT PVRSNLGSMP LKQWARFEEV RSSFTRWAAE DDICHDSDLM AEIEEDLLYA
     PYLERQEAEL RDLRAAETTE IPSWFEYSAL PGLSNEMVER LSRARPRSVA AAGRVAGITP
     SALATLVVNL RKQTNSRAA
//
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