ID M0PG71_9EURY Unreviewed; 294 AA.
AC M0PG71;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Succinate dehydrogenase and fumarate reductase iron-sulfur protein {ECO:0000313|EMBL:EMA68564.1};
GN ORFNames=C462_13446 {ECO:0000313|EMBL:EMA68564.1};
OS Halorubrum arcis JCM 13916.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1230455 {ECO:0000313|EMBL:EMA68564.1, ECO:0000313|Proteomes:UP000011528};
RN [1] {ECO:0000313|EMBL:EMA68564.1, ECO:0000313|Proteomes:UP000011528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13916 {ECO:0000313|EMBL:EMA68564.1,
RC ECO:0000313|Proteomes:UP000011528};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA68564.1}.
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DR EMBL; AOJJ01000082; EMA68564.1; -; Genomic_DNA.
DR RefSeq; WP_007996617.1; NZ_AOJJ01000082.1.
DR AlphaFoldDB; M0PG71; -.
DR STRING; 1230455.C462_13446; -.
DR PATRIC; fig|1230455.3.peg.2601; -.
DR Proteomes; UP000011528; Unassembled WGS sequence.
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 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; 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:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 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.
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 58..162
FT /note="Succinate dehydogenase/fumarate reductase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13085"
FT DOMAIN 199..273
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 34068 MW; 98E391A8BE592DD2 CRC64;
MSTQIPKQTE ESTETETEPA SKGDERRAEK RRRAADRREQ RQQEEAEKAA ADESTVELKV
FRYDPQVEGK QEPRFDTFHV PFTKGMTVLD ALMYARDTYD SSLTFRHSCR QAVCGSDAMF
VNGGQKLACK TQISDLDEPV RVEPLPHAEV TKDLVVDMEH FYDQMEAVEP YFQTNEYPDG
ELEEQRQDRE NREKIKMSTR CIWCGACMSS CNIAAGDNEY LGPAAINKAY RFAMDEREGE
DIKQKRLEII EQEHGVWRCQ TQFSCTEVCP KDIPLTEHIQ ELKREAVKNN LKFW
//
