ID A0A0B2JVL9_9FIRM Unreviewed; 330 AA.
AC A0A0B2JVL9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:KHM52385.1};
GN ORFNames=NZ47_05230 {ECO:0000313|EMBL:KHM52385.1};
OS Anaerovibrio lipolyticus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM52385.1, ECO:0000313|Proteomes:UP000030993};
RN [1] {ECO:0000313|EMBL:KHM52385.1, ECO:0000313|Proteomes:UP000030993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5S {ECO:0000313|EMBL:KHM52385.1,
RC ECO:0000313|Proteomes:UP000030993};
RX PubMed=23950883;
RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA Scollan N.D., Huws S.A., Newbold C.J.;
RT "Identification and characterization of three novel lipases belonging to
RT families II and V from Anaerovibrio lipolyticus 5ST.";
RL PLoS ONE 8:E69076-E69076(2013).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KHM52385.1}.
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DR EMBL; JSCE01000100; KHM52385.1; -; Genomic_DNA.
DR RefSeq; WP_039207187.1; NZ_JSCE01000100.1.
DR AlphaFoldDB; A0A0B2JVL9; -.
DR STRING; 82374.NZ47_05230; -.
DR eggNOG; COG0535; Bacteria.
DR Proteomes; UP000030993; Unassembled WGS sequence.
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; IPR034391; Cmo-like_SPASM_containing.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR017200; PqqE-like.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR027633; rSAM_NirJ2.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR04055; rSAM_NirJ2; 1.
DR PANTHER; PTHR11228; RADICAL SAM DOMAIN PROTEIN; 1.
DR PANTHER; PTHR11228:SF34; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE COFACTOR MODIFYING PROTEIN; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR SFLD; SFLDG01387; BtrN-like_SPASM_domain_contain; 1.
DR SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 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:UP000030993};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 1..211
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 330 AA; 37005 MW; F43D281E4AE5BB4C CRC64;
MIVSWNVTNA CNMFCDHCYR EAGCKAEEEL STEEAKTLLE QIARAGFKIM IFSGGEPLIR
PDILELVSYA TSLGLRSVFG TNGTLITLEM AQKLKAAGAM GMGISLDSMD KKKHNEFRKF
DGAWEGAVRG MRNCRAVGLP FQIHTTVMDW NNHELEAITD FAVAEGAVAH HFFFLVPAGR
AKTIEAESLR AEQYEETLTR IMKKQTEVDI ELKPTCAPQF MRIAAQMGIK TRFRRGCLAG
TAYCIISPRG KVQPCAYLNM ELGDVRETPF DEIWKNNEVL NTLRTLEYKG GCGECEFKRA
CGGCRARAAY YHDGDYMAEE PWCLYHGRKG
//
