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Database: UniProt
Entry: I5AVD9_EUBCE
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ID   I5AVD9_EUBCE            Unreviewed;       579 AA.
AC   I5AVD9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:EIM57762.1};
GN   ORFNames=EubceDRAFT1_1989 {ECO:0000313|EMBL:EIM57762.1};
OS   [Eubacterium] cellulosolvens 6.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM57762.1, ECO:0000313|Proteomes:UP000005753};
RN   [1] {ECO:0000313|EMBL:EIM57762.1, ECO:0000313|Proteomes:UP000005753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6 {ECO:0000313|EMBL:EIM57762.1,
RC   ECO:0000313|Proteomes:UP000005753};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., Johnson E.,
RA   Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EIM57762.1, ECO:0000313|Proteomes:UP000005753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6 {ECO:0000313|EMBL:EIM57762.1,
RC   ECO:0000313|Proteomes:UP000005753};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., Mukhopadhyay B.,
RA   Anderson I., Woyke T.;
RT   "Improved High-Quality Draft sequence of Eubacterium cellulosolvens 6.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CM001487; EIM57762.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5AVD9; -.
DR   STRING; 633697.EubceDRAFT1_1989; -.
DR   eggNOG; COG1032; Bacteria.
DR   HOGENOM; CLU_021572_1_0_9; -.
DR   OrthoDB; 9801424at2; -.
DR   Proteomes; UP000005753; 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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   CDD; cd02068; radical_SAM_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR025288; DUF4080.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR   PANTHER; PTHR43409:SF18; RADICAL SAM SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF13311; DUF4080; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005753}.
FT   DOMAIN          1..139
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          187..417
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   579 AA;  66731 MW;  9CBD34EB79672ABB CRC64;
     MKILLAALNA KYIHSNLAVR TLESYARTHL PKQEMPELEI CEYTINEQKD HILADIYGRN
     PDVITFSCYI WNMEMIFSLA KTLKLILPEV PVWLGGPEVS FDAPAILKEH PEIAGIMTGE
     GEATFAGLMK FFKEAGSGDA GLPETLTGIV FRRGTGEIVT APPTPPLDLD EIPFFYRDMA
     GEEGMEVFRH RIIYYESSRG CPFSCSYCLS SLREKVRFRS LPKVCEELQF FLDAGVPQVK
     FVDRTFNCNH RHAMGIWQYI REHDNKLTNF HFEIAADLLT DEEIDFLSTL RPGLVQLEIG
     VQSTNPDTLA AIDRVQNMDH LRSVTERIRG GKNIHQHLDL IAGLPHEDVV SFRRSFDEVY
     AMKPQQFQLG FLKVLKGSAM HRRAEEFGIV YHPEAPYEVI RTNWLSYRDV LYLKGVEEMT
     EVYYNSCQFV HTMEALTEEI GSAFDTYAAI ADWYRRQFPR DVQHSRLARF TILRDFIRDR
     FPARQKFYEG LLLLDLYLRE NAKSRPSWAP DPALWKSVFQ DYYREHAEGR LDRRMMHGEV
     FDVDVLGIGG SGPWPVVFDY RSRDPLTGNA QVIHVKTTK
//
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