ID A7HAF1_ANADF Unreviewed; 444 AA.
AC A7HAF1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ABS25697.1};
DE Flags: Precursor;
GN OrderedLocusNames=Anae109_1490 {ECO:0000313|EMBL:ABS25697.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25697.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS25697.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25697.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000769; ABS25697.1; -; Genomic_DNA.
DR RefSeq; WP_011985803.1; NC_009675.1.
DR AlphaFoldDB; A7HAF1; -.
DR STRING; 404589.Anae109_1490; -.
DR KEGG; afw:Anae109_1490; -.
DR eggNOG; COG2896; Bacteria.
DR HOGENOM; CLU_645348_0_0_7; -.
DR OrthoDB; 9764628at2; -.
DR Proteomes; UP000006382; 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; IPR007197; rSAM.
DR PANTHER; PTHR30352:SF23; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR SFLD; SFLDG01109; Uncharacterised_Radical_SAM_Su; 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};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 184..421
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48352 MW; C23700FCF71FF5B8 CRC64;
MPKLLFADDR GNVYDHPELD AAVRSGDAAT GTRERPIDLP EGASLCMLPG RRPVGIDPSS
GALVVLHEIK LGRRRVKPHA VGATLPPGYT RTFLPAAARA ALPTTGEAPI LPQWAYTAAA
LGPRGPVAWA LHTDRRSHWS PTAHSTEDLP ELVERTLEET DNPIYRQLAR CALEWRCFTA
QNTFYARDEG AIPASASCNA SCVGCLSEQQ EGMPPSSHER IARPPTAEEM AEVALRHLAR
ATGRIMVSFG QGCEGEPLTR WKEIERALRR VRAETRRGSL HANTNGSLPD ALGRLIDAGL
DSVRISTNSA SPDLYAAYYR PSGYGLADVV RSIRVAKERG AYVALNLLTF PGVTDREGEA
ERLCRLVAET GVDQVQTRPL ALDPDVYVEL SRGLGGGGPA LGIRRLVAEL KRARPGLVVG
NFSRARRERA KPERRARRGR PEAR
//
