ID A0A135VQF8_9ARCH Unreviewed; 324 AA.
AC A0A135VQF8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glycyl-radical enzyme activating protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AM325_05320 {ECO:0000313|EMBL:KXH74938.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-45.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706444 {ECO:0000313|EMBL:KXH74938.1, ECO:0000313|Proteomes:UP000070149};
RN [1] {ECO:0000313|EMBL:KXH74938.1, ECO:0000313|Proteomes:UP000070149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-45 {ECO:0000313|EMBL:KXH74938.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|ARBA:ARBA00009777}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH74938.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LRSL01000019; KXH74938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VQF8; -.
DR STRING; 1706444.AM325_05320; -.
DR Proteomes; UP000070149; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.80.30.10; pyruvate-formate lyase- activating enzyme; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR040074; BssD/PflA/YjjW.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02494; PFLE_PFLC; 1.
DR PANTHER; PTHR30352:SF4; PYRUVATE FORMATE-LYASE 2-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 1.
DR SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 16..298
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 47..75
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 76..105
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 324 AA; 36340 MW; C7E225DDF78D3001 CRC64;
MTTSGIITNI QRCSTEDGPG IRTTVFFKGC PMSCSWCHNI ETINPESTLV WYKVKCIGDQ
ACVRICPEDA LTLTPDGLKI DRERCVVCGT CEEACPTGAV KVMGKSWTSV DLVQELLKDK
VFFETSNGGV TLSGGEATFQ SKFALEVAKG LKDEGVHVAL DTCGYCSEKV LWDLLPYVDL
ILYDLKIMDP QKHKEYTGVP LDTVLTNAHI VAESGKPTWI RTPIIPEHTD DEENIRAIAR
FVLQHLPNVE RYDLLAFNRM CIDKYELFDL EYPLKDYDLV SVETMENLAQ VAREEGLSNV
VWSGMTKRSK KMNNMENQEI ETCG
//
