ID H6LFI0_ACEWD Unreviewed; 442 AA.
AC H6LFI0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative Fe-S oxidoreductase {ECO:0000313|EMBL:AFA49467.1};
GN OrderedLocusNames=Awo_c27140 {ECO:0000313|EMBL:AFA49467.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA49467.1, ECO:0000313|Proteomes:UP000007177};
RN [1] {ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFA49467.1, ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RX PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA Gottschalk G., Muller V.;
RT "An ancient pathway combining carbon dioxide fixation with the generation
RT and utilization of a sodium ion gradient for ATP synthesis.";
RL PLoS ONE 7:E33439-E33439(2012).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP002987; AFA49467.1; -; Genomic_DNA.
DR RefSeq; WP_014357065.1; NC_016894.1.
DR AlphaFoldDB; H6LFI0; -.
DR STRING; 931626.Awo_c27140; -.
DR KEGG; awo:Awo_c27140; -.
DR eggNOG; COG1964; Bacteria.
DR HOGENOM; CLU_023791_0_0_9; -.
DR OrthoDB; 9810775at2; -.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034474; Methyltransferase_Class_D.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43306; 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN DIMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43306:SF1; 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN DIMETHYLTRANSFERASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
DR SFLD; SFLDG01100; methyltransferase_(Class_D); 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 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:UP000007177};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 87..303
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 442 AA; 50049 MW; 3D2F678176477A1E CRC64;
MKRISTITQS LCPICLKKIN AIIWNENNET YMEKSCPDHG RFKALLWRGS ILRENWVRDK
IPTTIKNPNT MVEKGCPYDC GLCADHRQHT CTALIEVTQR CNLNCTFCFA NANNDKDQDL
SLETITAMYQ SVWKTSGNCN IQLSGGEPTL RDDLPEIIKL GHKIGFEFIQ LNTNGIRLAE
DEPYLKQLKE AGLDSVFLQF DGTNDEIYKK LRGKALFATK IKALENCRKY QIGVVLVPTL
VSAVNDTDLG NIIAFATSWL PTVRGVHMQP ASYFGRIPNL PVEEKRLTLG DIMDKIEVQT
NGRIKKETFT PPGCENARCS FHGNYIYEKN GDLTPLNNPS KCCKKETAEE GANKAKAHVA
RKWSTKDHPD ETAKPLDAWD EILARINQYT LSISAMAFQD VWNLDLERVK DCCIHVVDPN
GKLIPFCMYN LTNKEGESLY RK
//
