ID A0A0G3AH24_9ACTN Unreviewed; 256 AA.
AC A0A0G3AH24;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Fumarate reductase {ECO:0000313|EMBL:AKJ11030.1};
GN ORFNames=ABB07_13670 {ECO:0000313|EMBL:AKJ11030.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ11030.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ11030.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
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DR EMBL; CP011497; AKJ11030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3AH24; -.
DR STRING; 665007.ABB07_13670; -.
DR PATRIC; fig|665007.5.peg.2952; -.
DR Proteomes; UP000035366; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
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; IPR012675; Beta-grasp_dom_sf.
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; PTHR11921:SF35; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
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.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00022714};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 6..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 256 AA; 28939 MW; BDBC4C811784D113 CRC64;
MSSYEARFKV WRGDAEGGGL EDFEVEVNDG EVVLDIIHRL QATQAPDLAV RWNCKAGKCG
SCSAEINGRP RLMCMTRMSV FSREETITVT PLRAFPVVRD LVTDVGFNYQ KAREVPAFVP
PAGLGPGEYR MMQEDVDRSQ EFRKCIECFL CQDTCHVVRD HEENKKAFAG PRFLMRIAEL
DMHPLDSAAD TGLDRKRTAQ DEHGLGYCNI TKCCTEVCPE GIKITDNALI PMKERAVDRK
YDPLVWLGSK IRRRSS
//
