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Database: UniProt
Entry: Q2LTL5_SYNAS
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ID   Q2LTL5_SYNAS            Unreviewed;       452 AA.
AC   Q2LTL5;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:ABC77428.1};
GN   ORFNames=SYN_02176 {ECO:0000313|EMBL:ABC77428.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77428.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC77428.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC77428.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP000252; ABC77428.1; -; Genomic_DNA.
DR   RefSeq; WP_011417450.1; NC_007759.1.
DR   AlphaFoldDB; Q2LTL5; -.
DR   KEGG; sat:SYN_02176; -.
DR   eggNOG; COG1032; Bacteria.
DR   HOGENOM; CLU_021572_4_3_7; -.
DR   InParanoid; Q2LTL5; -.
DR   OrthoDB; 9804952at2; -.
DR   Proteomes; UP000001933; 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:InterPro.
DR   CDD; cd01335; Radical_SAM; 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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
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; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT   DOMAIN          9..188
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          206..436
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   452 AA;  52246 MW;  85D432C0213F20BD CRC64;
     MNTNVLLINP WIYDFAAYDF WSKPLGLLYM AGILRKNSIG VQLIDCMNPC HPGLDGEKHI
     KKPRRKAFGQ GHYPKERIPK PEPLQDFPRN YYRYGITPRI FRHELNSRTP PDLIMITSLM
     TYWYPGVFDV IRIVREIFPG IPVILGGIYA TLCPEHALQS GADYVLTGEG ELQIRFIIED
     LLHRKIEYLP VLSELDSLPY PAFDLLPYKE QLPIMTSRGC PFRCTYCASH ILNSSFRRRS
     PNHVAEEITF WNRNFGIRHF SFYDDAFLIN SEDTAIPLMK EIIRRDLSCQ FHCPNGLHLR
     TITAKISRLM YRSGFRTLRF GFETSDFERQ LRTGGKVSNE HLHSAFSYLK EAGYAPQDIG
     LYLLCGLPEQ DAREVEESIR FVLSLGARPI LAEFSPIPGT ALWNKAVETS SYDIANEPLF
     HNNSLLPCRH EHFSCEDYRK LKNTIRRGRS DT
//
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