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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//