ID A0A087AYN0_9BIFI Unreviewed; 233 AA.
AC A0A087AYN0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase activating protein {ECO:0000313|EMBL:KFI63880.1};
GN ORFNames=BCUN_1492 {ECO:0000313|EMBL:KFI63880.1};
OS Bifidobacterium cuniculi.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI63880.1, ECO:0000313|Proteomes:UP000029067};
RN [1] {ECO:0000313|EMBL:KFI63880.1, ECO:0000313|Proteomes:UP000029067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI63880.1,
RC ECO:0000313|Proteomes:UP000029067};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KFI63880.1}.
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DR EMBL; JGYV01000006; KFI63880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087AYN0; -.
DR STRING; 1688.BCUN_1492; -.
DR eggNOG; COG0602; Bacteria.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000029067; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012837; NrdG.
DR InterPro; IPR034457; Organic_radical-activating.
DR NCBIfam; TIGR02491; NrdG; 1.
DR PANTHER; PTHR30352:SF2; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR SFLD; SFLDG01063; activating_enzymes__group_1; 1.
DR SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT REGION 13..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 26684 MW; C6F76277E793AC1D CRC64;
MVQAAPRHDF VKTKEYRGPS VPSPLTNNPR AGQWTNRMSH NMIADYKRFL MTDGEGIRCS
LYVSGCPFHC EECYNSSIWD FQAGHEYNDK LEAQIMDDLS QSFVQGITFL GGEPLLNTGV
LLPLTRRIRE RFGHTKDIWC WTGYTWEELM RDGETQDKLD LLGQVDILVD GRYIKTLHDS
LLQFRGSSNQ RIIDVPASLE QGKVVIWSKL HDQERFIPEI YGHERAAGEG DAS
//