ID A0A0U4W329_9BACT Unreviewed; 366 AA.
AC A0A0U4W329;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyruvate formate lyase-activating protein {ECO:0000313|EMBL:BAU23498.1};
GN ORFNames=THC_1119 {ECO:0000313|EMBL:BAU23498.1};
OS Caldimicrobium thiodismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23498.1, ECO:0000313|Proteomes:UP000068196};
RN [1] {ECO:0000313|EMBL:BAU23498.1, ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|EMBL:BAU23498.1,
RC ECO:0000313|Proteomes:UP000068196};
RX PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring, and emended description of the genus
RT Caldimicrobium.";
RL Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN [2] {ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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; AP014945; BAU23498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4W329; -.
DR STRING; 1653476.THC_1119; -.
DR KEGG; cthi:THC_1119; -.
DR OrthoDB; 37798at2; -.
DR Proteomes; UP000068196; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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; 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; PF13353; Fer4_12; 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.
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:BAU23498.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50}; Pyruvate {ECO:0000313|EMBL:BAU23498.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068196};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 131..356
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 148
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 152
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 155
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 366 AA; 41213 MW; F171A68654479530 CRC64;
MSLKTCLICG ERKILSSFIG ICKDCLRDNF NRAKPFLEKA HKESRKAFSL PEETPTDKEG
ISCPICARGC RIAEGEYGYC GLRKILKGKL LGPKIREARV SWYLDPLPTN CVADWICPGG
TGCGYPKFAY RSGPEYGYYN LAVFFEACNL NCLYCQNWHF KYATFATRYK TLEEFLEAIT
PQVACICFFG GDPSPQAPFA IKASFEALKN KKGKILRICW ETNGHFSPHL LPKVIETSLV
SGGIIKFDLK ALTPEIYFAL TGGSLNPVLE NFKKVAEYFK ERPEVSLLTA STLLVPGYVE
EEEVEKIAQF IAEINPQIPY RILAFSPQFY MKDLPLISKE VAYRALERAK KAGLKRVSLG
NEHLLK
//
