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Database: UniProt
Entry: D9PZN1_ACIS3
LinkDB: D9PZN1_ACIS3
Original site: D9PZN1_ACIS3 
ID   D9PZN1_ACIS3            Unreviewed;       387 AA.
AC   D9PZN1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Predicted Fe-S oxidoreductase {ECO:0000313|EMBL:ADL18519.1};
GN   OrderedLocusNames=ASAC_0111 {ECO:0000313|EMBL:ADL18519.1};
OS   Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS   345-15).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18519.1, ECO:0000313|Proteomes:UP000000346};
RN   [1] {ECO:0000313|EMBL:ADL18519.1, ECO:0000313|Proteomes:UP000000346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC   {ECO:0000313|Proteomes:UP000000346};
RX   PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA   Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT   a new order, Acidilobales, and suggests an important ecological role in
RT   terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP001742; ADL18519.1; -; Genomic_DNA.
DR   RefSeq; WP_013266031.1; NC_014374.1.
DR   AlphaFoldDB; D9PZN1; -.
DR   STRING; 666510.ASAC_0111; -.
DR   GeneID; 9498324; -.
DR   KEGG; asc:ASAC_0111; -.
DR   eggNOG; arCOG00940; Archaea.
DR   HOGENOM; CLU_009273_4_0_2; -.
DR   InParanoid; D9PZN1; -.
DR   OrthoDB; 30736at2157; -.
DR   Proteomes; UP000000346; 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   CDD; cd21123; SPASM_MftC-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR017200; PqqE-like.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR04053; TIGR04053 family radical SAM/SPASM domain-containing protein; 1.
DR   PANTHER; PTHR11228; RADICAL SAM DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR11228:SF34; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE COFACTOR MODIFYING PROTEIN; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR   SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
DR   SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
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:UP000000346};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          10..234
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   387 AA;  42907 MW;  76612F9373658C46 CRC64;
     MSRRGRWPFE EKPLLVFWET TKACPLACIH CRAEAITRPL PGELSHAEGL ELVRQVAEFG
     RPYPILVFTG GDPLSREDIW ELVDEAHSLG VPVAMAPSPS RALLDNLDRI ASGKVSAVSI
     SIDHPSPEVH DKVRRYQGSW EAGVTAIREL IRRGVKVQVN TAVMRSTVDG LPGMVKLLKD
     LGVDVWEVFY LVPVGRAEAR EDLTPQEWED VSAFLYEASR YGINVRTSEG PMFRRVSLLL
     NYARSRNLEP SKLVKLGDLY LRLTGQLRAL LGEPGEEARF ETSGTRDGKG IAFISHDGMV
     YPSGFLPVPV GNVRRERLVD IYRRSRLMVS LREASFRGRC GSCEFKEICG GSRARAFAYS
     GDPLGEDPAC PYVPGSLGVN VKEVMAP
//
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