ID B4S3W0_PROA2 Unreviewed; 340 AA.
AC B4S3W0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Succinate dehydrogenase and fumarate reductase iron-sulfur protein {ECO:0000313|EMBL:ACF45306.1};
GN OrderedLocusNames=Paes_0249 {ECO:0000313|EMBL:ACF45306.1};
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF45306.1, ECO:0000313|Proteomes:UP000002725};
RN [1] {ECO:0000313|EMBL:ACF45306.1, ECO:0000313|Proteomes:UP000002725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001108; ACF45306.1; -; Genomic_DNA.
DR RefSeq; WP_012504843.1; NC_011059.1.
DR AlphaFoldDB; B4S3W0; -.
DR STRING; 290512.Paes_0249; -.
DR KEGG; paa:Paes_0249; -.
DR eggNOG; COG0479; Bacteria.
DR HOGENOM; CLU_044838_3_1_10; -.
DR Proteomes; UP000002725; 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: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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002725}.
FT DOMAIN 9..105
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 340 AA; 38990 MW; 0767307065227F3F CRC64;
MGEHKEEMRD ITFRVLRFNP QIDNKPYFDD YTIPVEKGIT VLRALNYIKE HVDASVSFRA
FCQAGICGSC GMRINGISKL ACTTQVWDEI ERCKVANVIK VEPLRNMPHV KDLIVDMDPM
VEKMKQYSNW IESTMPESQM GDKEFLISEE EFQEYDKATD CILCASCMSE CSILRANKEY
VAPAILLKSH RMNVDSRDGS HDKRMAELVK DHGVWDCTHC YRCQETCVKN IPIMDAIHGV
REDALAARGV KDSSGARHAE AFMDDISKKG KLVESTLPVR TNGLNWTLKN LLPMAFKMVM
KRRTPPPPPL VKPSKGIKKF REEFNEMTEH VKRDQKDNHK
//
