ID D9Q2H2_ACIS3 Unreviewed; 362 AA.
AC D9Q2H2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Pyruvate-formate lyase-activating enzyme, PflA {ECO:0000313|EMBL:ADL19510.1};
DE EC=1.97.1.4 {ECO:0000313|EMBL:ADL19510.1};
GN OrderedLocusNames=ASAC_1105 {ECO:0000313|EMBL:ADL19510.1};
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:ADL19510.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL19510.1, 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|PIRSR:PIRSR004869-50};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|PIRSR:PIRSR004869-50};
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DR EMBL; CP001742; ADL19510.1; -; Genomic_DNA.
DR RefSeq; WP_013267022.1; NC_014374.1.
DR AlphaFoldDB; D9Q2H2; -.
DR STRING; 666510.ASAC_1105; -.
DR GeneID; 9499353; -.
DR KEGG; asc:ASAC_1105; -.
DR eggNOG; arCOG00946; Archaea.
DR HOGENOM; CLU_044176_1_0_2; -.
DR InParanoid; D9Q2H2; -.
DR OrthoDB; 5682at2157; -.
DR Proteomes; UP000000346; Chromosome.
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:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR027596; AmmeMemoSam_rS.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR04337; AmmeMemoSam_rS; 1.
DR PANTHER; PTHR30352:SF20; MOAA_NIFB_PQQE FAMILY PROTEIN; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004869; PflX_prd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01101; Uncharacterised_Radical_SAM_Su; 1.
DR SMART; SM00729; Elp3; 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, ECO:0000256|PIRSR:PIRSR004869-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR004869-
KW 50}; Lyase {ECO:0000313|EMBL:ADL19510.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50};
KW Oxidoreductase {ECO:0000313|EMBL:ADL19510.1};
KW Pyruvate {ECO:0000313|EMBL:ADL19510.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 77..294
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
SQ SEQUENCE 362 AA; 41367 MW; 1E675A4B583CD8B6 CRC64;
MNNEQKPNLR EAKFWEPLAD RKGWVKCNLC HRRCLIAPGR WGACGVRRNL DGRLYTYVYG
LLTAYNLDPI EKKPLSHFNP GSEVLSISTV GCDFYCQFCQ NWEISQSRLE KGLYGEYRSP
DDVVRDAINV GADGISYTYN EPTIMYEYMY DVAVRAKKFG LFNTMVTNGY MTPEAVDEIG
SYMDAATVDF KGGGNKEFYR KFMGVPDPEP IFETLKAMKE KGIWIEITNL VVPKYGDNED
DIRKLARWIV DNLGDRVPFH LLKFYPEYKM IDLESTPVKT LERLAKAAKE EGLKYVYIGN
VPGHPLEHTY CPSCGYPVIE RYGFYVTAWR LTKDNRCPRC GAKIDIVGAF RNKAGAASIP
LM
//
