ID Q97K49_CLOAB Unreviewed; 470 AA.
AC Q97K49;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AAK79046.1};
GN OrderedLocusNames=CA_C1072 {ECO:0000313|EMBL:AAK79046.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79046.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK79046.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AE001437; AAK79046.1; -; Genomic_DNA.
DR PIR; C97032; C97032.
DR RefSeq; NP_347706.1; NC_003030.1.
DR RefSeq; WP_010964387.1; NC_003030.1.
DR AlphaFoldDB; Q97K49; -.
DR STRING; 272562.CA_C1072; -.
DR GeneID; 44997585; -.
DR KEGG; cac:CA_C1072; -.
DR PATRIC; fig|272562.8.peg.1282; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_581005_0_0_9; -.
DR OrthoDB; 9801424at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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 Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43409:SF7; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE; 1.
DR PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 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:UP000000814};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 3..145
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 191..428
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 470 AA; 53131 MW; 7897C01D31717015 CRC64;
MKKHIALIFT PINKKYKDAL THYAPPLGLV ALANYISERL QNVRISILDG SVTHSMEDII
KFIEDEKPDI VAQSVQLISY ENSLVIAKSA HNIGSINVLG GQHATQMADA IIFRQQGLID
YVSIEDGEES LLGLLEERDI SEIPNLVFMK DGKINRTKYF QLDLKNAPKL DYSIVDFKPY
QKLLNESNFT NPNPINNYLR VYSHKGCGNR KNSVGCVFCG RADKGVRFKS PEKFWEDIKI
CADEFKADYI FDVGDDFLYN HDWVSKVAEI KPDIRKKFEL GIFARANRVN LSIAKKLKKI
GVTDVVIGFE SGDEEVLRRC NKRDTSTETS LIAADALATA GIDITASFVL GLPGENSESL
KKTIKCAEKV VNIITEKLGR PPREMVGNLI EPSPGSIAYN QLLKAYPGKY YLNDYVPLDE
MQRDYFKYYF GLDSLKSYLE FRKELNKAAQ EIHGLVSFSD SQGWLEDEFV
//
