ID Q8ZV55_PYRAE Unreviewed; 364 AA.
AC Q8ZV55;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Pyruvate formate-lyase activating enzyme homolog {ECO:0000313|EMBL:AAL64201.1};
GN OrderedLocusNames=PAE2451 {ECO:0000313|EMBL:AAL64201.1};
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL64201.1, ECO:0000313|Proteomes:UP000002439};
RN [1] {ECO:0000313|EMBL:AAL64201.1, ECO:0000313|Proteomes:UP000002439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC IM2 {ECO:0000313|Proteomes:UP000002439};
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64201.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZV55; -.
DR STRING; 178306.PAE2451; -.
DR EnsemblBacteria; AAL64201; AAL64201; PAE2451.
DR KEGG; pai:PAE2451; -.
DR PATRIC; fig|178306.9.peg.1825; -.
DR eggNOG; arCOG00936; Archaea.
DR HOGENOM; CLU_044176_0_0_2; -.
DR InParanoid; Q8ZV55; -.
DR Proteomes; UP000002439; 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; IPR034457; Organic_radical-activating.
DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352:SF22; PYRUVATE FORMATE-LYASE ACTIVATING ENZYME HOMOLOG; 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 SUPFAM; SSF102114; Radical SAM enzymes; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50}; Pyruvate {ECO:0000313|EMBL:AAL64201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002439};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 143..295
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
FT BINDING 147
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 151
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 154
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 364 AA; 40273 MW; B014CB250331C806 CRC64;
MGFCKLCGKS SITISNFLGV CVDCLRGRPR QALEIAKRAH IISRGKFNLP IEAPTKGVPC
GICGRGCLIP EGGVGYCGLV RNIGGRLVRP GGEISKGVLS YYYDPIPTNC VADWVCPATT
GRGYPKFSKS PWGEAGYYNL AVFYGACGLD CLYCQNWQYR EYPARPRLVA VEELEKAMNR
RVTCVCFFGG DPGPQTVHAL MVAKKAAEKG VRVCWETSGQ LAPHLLDRIV DFSLRTGGIV
KFDLKAFTPS VYKALTDGEV DVALRNFKVA ARRFRERPEV PLVVASILLV PGYVDAVEVD
LLTKFIARID PEIPTRFLAF HPDYLLRDLP PTSIKHAEEA VRIAKENGLM EVSIRNQWLL
GDYY
//
