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Database: UniProt
Entry: A0A1H1MU27_9ACTN
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ID   A0A1H1MU27_9ACTN        Unreviewed;       190 AA.
AC   A0A1H1MU27;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|ARBA:ARBA00014281, ECO:0000256|PIRNR:PIRNR000368};
DE            EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN   ORFNames=SAMN04489857_1572 {ECO:0000313|EMBL:SDR90206.1};
OS   Parafannyhessea umbonata.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Parafannyhessea.
OX   NCBI_TaxID=604330 {ECO:0000313|EMBL:SDR90206.1, ECO:0000313|Proteomes:UP000199480};
RN   [1] {ECO:0000313|Proteomes:UP000199480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22620 {ECO:0000313|Proteomes:UP000199480};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00003852,
CC       ECO:0000256|PIRNR:PIRNR000368}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC         methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC         + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC         Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC         Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC         Evidence={ECO:0000256|ARBA:ARBA00000544};
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|ARBA:ARBA00009777, ECO:0000256|PIRNR:PIRNR000368}.
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DR   EMBL; LT629759; SDR90206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1MU27; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000199480; Chromosome i.
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   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
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; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 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|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000368};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ   SEQUENCE   190 AA;  20960 MW;  A9183AD1754445E5 CRC64;
     MNYANIKYCD IANGIGVRTT VFVSGCRLHC KGCFNAEAWS FSAGKPFDRE VEDKVLESLR
     PSYVNGLSVL GGEPTEPENV AALAPFLERV RAELPEKDIW MYSGRTWEQL TGDGDHASPD
     MDRVLSCLDV LVDGPFVQDL YDISLRFRGS SNQRLIDVPA TLKAHADGTL SGANDVVEWV
     DDPVFSTHSM
//
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