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Database: UniProt
Entry: A0A0R2FCU0_9LACO
LinkDB: A0A0R2FCU0_9LACO
Original site: A0A0R2FCU0_9LACO 
ID   A0A0R2FCU0_9LACO        Unreviewed;       194 AA.
AC   A0A0R2FCU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE            EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN   ORFNames=FD14_GL002326 {ECO:0000313|EMBL:KRN26259.1};
OS   Secundilactobacillus similis DSM 23365 = JCM 2765.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN26259.1, ECO:0000313|Proteomes:UP000051442};
RN   [1] {ECO:0000313|EMBL:KRN26259.1, ECO:0000313|Proteomes:UP000051442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN26259.1,
RC   ECO:0000313|Proteomes:UP000051442};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- FUNCTION: Activation of anaerobic ribonucleoside-triphosphate reductase
CC       under anaerobic conditions by generation of an organic free radical,
CC       using S-adenosylmethionine and reduced flavodoxin as cosubstrates to
CC       produce 5'-deoxy-adenosine. {ECO:0000256|PIRNR:PIRNR000368}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000256|PIRNR:PIRNR000368}.
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:KRN26259.1}.
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DR   EMBL; AYZM01000038; KRN26259.1; -; Genomic_DNA.
DR   RefSeq; WP_054732663.1; NZ_BBAD01000002.1.
DR   AlphaFoldDB; A0A0R2FCU0; -.
DR   STRING; 1423804.FD14_GL002326; -.
DR   PATRIC; fig|1423804.4.peg.2519; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000051442; 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   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   PIRSF; PIRSF000368; NrdG; 1.
DR   SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR   SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE   3: Inferred from homology;
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   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000368};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051442};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ   SEQUENCE   194 AA;  22193 MW;  33B3DDC82B566A50 CRC64;
     MTTESVKLPR NPEPKEWLAS ELSDQRIASY KPFNFVDGEG VRCSLYVSGC KFNCPGCYNK
     VAQNFHFGQP YTQELEDQII ADLGQSYVQG LTLLGGEPFL NTQVCLKLCR RVREEFGDTK
     DIWSWTGYTW DELKQESEDK RELLQLLDIL VDGRFLQAKM DLTLQFRGSS NQRIINVPAS
     LATGDVVLWD KLIK
//
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