ID A2SPR0_METLZ Unreviewed; 481 AA.
AC A2SPR0;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Thiol-driven fumarate reductase, iron-sulfur protein {ECO:0000313|EMBL:ABN06316.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:ABN06316.1};
GN OrderedLocusNames=Mlab_0139 {ECO:0000313|EMBL:ABN06316.1};
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358 {ECO:0000313|EMBL:ABN06316.1, ECO:0000313|Proteomes:UP000000365};
RN [1] {ECO:0000313|EMBL:ABN06316.1, ECO:0000313|Proteomes:UP000000365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z {ECO:0000313|Proteomes:UP000000365};
RX PubMed=21304657; DOI=10.4056.sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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DR EMBL; CP000559; ABN06316.1; -; Genomic_DNA.
DR RefSeq; WP_011832517.1; NC_008942.1.
DR AlphaFoldDB; A2SPR0; -.
DR STRING; 410358.Mlab_0139; -.
DR GeneID; 4796037; -.
DR KEGG; mla:Mlab_0139; -.
DR eggNOG; arCOG00333; Archaea.
DR eggNOG; arCOG00963; Archaea.
DR HOGENOM; CLU_023081_2_0_2; -.
DR OrthoDB; 42878at2157; -.
DR Proteomes; UP000000365; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR NCBIfam; TIGR00384; dhsB; 1.
DR PANTHER; PTHR32479; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR32479:SF17; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ABN06316.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000365}.
FT DOMAIN 1..88
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 120..151
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 171..202
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 481 AA; 52984 MW; B02C3A08E920DD71 CRC64;
MKVTISRFDP ATGEPPKFVE YDVSVKDSAR VLNVLDAVHD TIDPEFAYRH CCRGGQCGSC
AVRVNGEPVL ACMQEAREGD IIEPLELPRI RDLVTDIAPV MAQMAWMNSG CDCTPVTQQE
IEEMKPLREC IECYSCISSC PAIAASDYKG PTIMRQEQRL NLDPRDKGDR ILEAIDKGLF
SCTTCHKCVE VCPKEIETPR KAIEKLRAEA AKRGLSLPAH KALASLIEKT GRSIERKEPT
FLERVPDVIE PEGEVRATVG FFVGCMFNGR VIQPALDAME VLRKNGIRVI IPKDQVCCGS
PLIRTGLCGF IPELQKRNID AFVKAGVDTV LTICAGCGST LKNDYDTPFR VVDITEFLCE
LGFEIPEKVE GTYTYHDPCH LLRGQGISEQ PRILLNSVAE KFVEMPARCC GAGGGVKSGL
PEQAAAIGAV RAEMVKETGA DYIVTVCPFC EFHLHQVTGL PVKNIATLML EGYRKQEKKI
N
//
