ID A0A0L9TJ32_PHAAN Unreviewed; 725 AA.
AC A0A0L9TJ32;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain domain-containing protein {ECO:0000259|SMART:SM01228};
GN ORFNames=LR48_Vigan01g011900 {ECO:0000313|EMBL:KOM30565.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM30565.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC {ECO:0000256|ARBA:ARBA00002739}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
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DR EMBL; CM003371; KOM30565.1; -; Genomic_DNA.
DR RefSeq; XP_017438496.1; XM_017583007.1.
DR AlphaFoldDB; A0A0L9TJ32; -.
DR STRING; 3914.A0A0L9TJ32; -.
DR EnsemblPlants; KOM30565; KOM30565; LR48_Vigan01g011900.
DR GeneID; 108344573; -.
DR Gramene; KOM30565; KOM30565; LR48_Vigan01g011900.
DR KEGG; var:108344573; -.
DR OMA; CNPAMGG; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000053144; Chromosome 1.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 613..684
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 725 AA; 81512 MW; 8E2CCE7305922195 CRC64;
MATAPLTLHL CRFSRNLCTK LFLTPSPDLP NPRRVTFRRK FRRQISFSSS FSRRFCASST
SRVVDCESGV VDEKYDVIVV GGGHAGCEAA LASARLGART LLLTLNIDRI AWQPCNPAVG
GPAKSQLVHE VDALGGEIGK IADRCYLQKR VLNVSRGPAV RALRAQTDKR EYAWQMKNVV
ESTPNLSIRE AMVTDILLGK NDNVEGVCTF FGMKFYAPSI ILTTGTFMSG KIWVGRTSMP
AGRAGESASL GLTENLQQLG FETDRLKTGT PARVDIRTVN FSVLEPQRGD EEVSWFSFDP
EVHIEREQMC CYLTRTTSTT HQIIRENLHE TPTYGGWVEA KGPRYCPSIE DKIVRFQDKE
SHQIFLEPEG RNVPELYVQG FSTGLPERLQ LPLLRTLPGL EKCSMLRPAY AVEYDYLPAH
QCARSLMTKK IQGLFFSGQI NGTTGYEEAA AQGIISGINA ARHADDKPLI VLERESSYIG
TLIDDLVTKD LREPYRVLTS RSEHRLLLRS DNADSRLTPL GHEIGLIDDR RWKLYQDKQD
RISREKKRLK SVRISGMDLA AEVTSLSGQP VKDSSTLESL LKKPHIQYEI LDKHGFGDKS
LSRMEKECVE IDIKYEGFIL RQQSQLQQLV AQHHRPLPED LDYYAMTTLS HEAREKLSKV
RPQTIGQASR VGGVSPADIT ALLIVLEARR RKAQEQRRYK MMNAVKENNQ VEKPEVSLTE
KVSSG
//
