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Database: UniProt
Entry: H9ULE2_SPIAZ
LinkDB: H9ULE2_SPIAZ
Original site: H9ULE2_SPIAZ 
ID   H9ULE2_SPIAZ            Unreviewed;       252 AA.
AC   H9ULE2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Anaerobic ribonucleoside-triphosphate reductase activating protein {ECO:0000313|EMBL:AFG38335.1};
GN   OrderedLocusNames=Spiaf_2302 {ECO:0000313|EMBL:AFG38335.1};
OS   Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38335.1, ECO:0000313|Proteomes:UP000007383};
RN   [1] {ECO:0000313|Proteomes:UP000007383}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC   {ECO:0000313|Proteomes:UP000007383};
RX   PubMed=23991249; DOI=10.4056/sigs.3607108;
RA   Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT   type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT   Rift.";
RL   Stand. Genomic Sci. 8:165-176(2013).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP003282; AFG38335.1; -; Genomic_DNA.
DR   RefSeq; WP_014456317.1; NC_017098.1.
DR   AlphaFoldDB; H9ULE2; -.
DR   STRING; 889378.Spiaf_2302; -.
DR   KEGG; sfc:Spiaf_2302; -.
DR   PATRIC; fig|889378.3.peg.2274; -.
DR   eggNOG; COG1180; Bacteria.
DR   HOGENOM; CLU_078147_2_1_12; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000007383; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic 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; IPR012840; NrdG2.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR02495; NrdG2; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01094; Uncharacterised_Radical_SAM_Su; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 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:UP000007383};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          22..243
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   252 AA;  27286 MW;  99B12B2A4FA377D9 CRC64;
     MGRRGPEVSL KRLGLQATTL LDYPGKVAAM VFTMGCPLRC PYCHNPQLVH GSPPAGFLAR
     EEVLRRLARR RHLLQGVVIT GGEPLRHHDI GGLLDDVHAL GLPVKLDTCG WYPAALAGVL
     EHPGLQYVAM DIKTLPEHYG RVAAGRGLGG TVLSRSPAIR ESVAVLRNWR DAQPERGLEY
     RTVCAPGVVD PGDLAGIARM LQPGDRWRLS QFQPGSCLDP TWNARTPFDT AVLEQAAAAA
     CRRGVDAWTV GV
//
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