ISF_METTE
ID ISF_METTE Reviewed; 191 AA.
AC Q50562;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Iron-sulfur flavoprotein;
DE Short=Isf;
GN Name=isf;
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, FMN BINDING,
RP IRON-SULFUR CLUSTER, AND SUBUNIT.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8798638; DOI=10.1074/jbc.271.39.24023;
RA Latimer M.T., Painter M.H., Ferry J.G.;
RT "Characterization of an iron-sulfur flavoprotein from Methanosarcina
RT thermophila.";
RL J. Biol. Chem. 271:24023-24028(1996).
RN [2]
RP FUNCTION.
RX PubMed=9756881; DOI=10.1074/jbc.273.41.26462;
RA Becker D.F., Leartsakulpanich U., Surerus K.K., Ferry J.G., Ragsdale S.W.;
RT "Electrochemical and spectroscopic properties of the iron-sulfur
RT flavoprotein from Methanosarcina thermophila.";
RL J. Biol. Chem. 273:26462-26469(1998).
RN [3]
RP IRON-SULFUR CLUSTER BINDING AT CYS-47; CYS-50; CYS-53 AND CYS-59, AND
RP MUTAGENESIS OF CYS-16; CYS-47; CYS-50; CYS-53; CYS-59 AND CYS-179.
RX PubMed=10986231; DOI=10.1128/jb.182.19.5309-5316.2000;
RA Leartsakulpanich U., Antonkine M.L., Ferry J.G.;
RT "Site-specific mutational analysis of a novel cysteine motif proposed to
RT ligate the 4Fe-4S cluster in the iron-sulfur flavoprotein of the
RT thermophilic methanoarchaeon Methanosarcina thermophila.";
RL J. Bacteriol. 182:5309-5316(2000).
CC -!- FUNCTION: Redox-active protein probably involved in electron transport
CC during fermentation of acetate to methane.
CC {ECO:0000269|PubMed:9756881}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Note=Binds 1 FMN per subunit.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8798638}.
CC -!- MISCELLANEOUS: The electrons derived from oxidation of the carbonyl
CC group of acetate flow from ferredoxin to the 4Fe-4S cluster and then to
CC the FMN cofactor.
CC -!- SIMILARITY: Belongs to the SsuE family. Isf subfamily. {ECO:0000305}.
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DR EMBL; U50189; AAC45465.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50562; -.
DR SMR; Q50562; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Flavoprotein; FMN; Iron; Iron-sulfur;
KW Metal-binding.
FT CHAIN 1..191
FT /note="Iron-sulfur flavoprotein"
FT /id="PRO_0000332945"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT MUTAGEN 16
FT /note="C->S: Unmodified 4Fe-4S-cluster properties in
FT electron paramagnetic resonance."
FT /evidence="ECO:0000269|PubMed:10986231"
FT MUTAGEN 47
FT /note="C->S: Modified 4Fe-4S-cluster properties in electron
FT paramagnetic resonance."
FT /evidence="ECO:0000269|PubMed:10986231"
FT MUTAGEN 50
FT /note="C->A: Formation of a 3Fe-4S cluster in place of the
FT 4Fe-4S cluster."
FT /evidence="ECO:0000269|PubMed:10986231"
FT MUTAGEN 53
FT /note="C->S: Modified 4Fe-4S-cluster properties in electron
FT paramagnetic resonance."
FT /evidence="ECO:0000269|PubMed:10986231"
FT MUTAGEN 59
FT /note="C->A: Formation of a 3Fe-4S cluster in place of the
FT 4Fe-4S cluster."
FT /evidence="ECO:0000269|PubMed:10986231"
FT MUTAGEN 179
FT /note="C->S: Unmodified 4Fe-4S-cluster properties in
FT electron paramagnetic resonance."
FT /evidence="ECO:0000269|PubMed:10986231"
SQ SEQUENCE 191 AA; 20921 MW; 0244D6DE7CF9AFAC CRC64;
MKITGISGSP RKGQNCEKII GAALEVAKER GFETDTVFIS NEEVAPCKAC GACRDQDFCV
IDDDMDEIYE KMRAADGIIV AAPVYMGNYP AQLKALFDRS VLLRRKNFAL KNKVGAALSV
GGSRNGGQEK TIQSIHDWMH IHGMIVVGDN SHFGGITWNP AEEDTVGMQT VSETAKKLCD
VLELIQKNRD K