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Database: UniProt
Entry: A0A3N2PEQ9_9ACTN
LinkDB: A0A3N2PEQ9_9ACTN
Original site: A0A3N2PEQ9_9ACTN 
ID   A0A3N2PEQ9_9ACTN        Unreviewed;       253 AA.
AC   A0A3N2PEQ9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Succinate dehydrogenase/fumarate reductase iron-sulfur subunit {ECO:0000313|EMBL:ROT33195.1};
GN   ORFNames=EF879_08765 {ECO:0000313|EMBL:ROT33195.1};
OS   Micromonospora sp. HM5-17.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2487710 {ECO:0000313|EMBL:ROT33195.1, ECO:0000313|Proteomes:UP000281230};
RN   [1] {ECO:0000313|EMBL:ROT33195.1, ECO:0000313|Proteomes:UP000281230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM5-17 {ECO:0000313|EMBL:ROT33195.1,
RC   ECO:0000313|Proteomes:UP000281230};
RA   Thawai C.;
RT   "Micromonospora sp. HM5-17, a new actinomycetes isolated from a hot spring
RT   soil.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
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:ROT33195.1}.
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DR   EMBL; RJWA01000002; ROT33195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2PEQ9; -.
DR   OrthoDB; 9804391at2; -.
DR   Proteomes; UP000281230; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   PANTHER; PTHR11921:SF41; 4FE-4S FERREDOXIN IRON-SULFUR BINDING DOMAIN PROTEIN; 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; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281230}.
FT   DOMAIN          150..179
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   253 AA;  26821 MW;  8FE9CA6720227BBE CRC64;
     MNLTLRIWRQ KGPDDPGRMV TYPVTDVSPD MSFLEMLDVL NEQLTLAGDD PVAFDHDCRE
     GICGACGMVI NGVAHGPEKA TTVCQLHMRH FSDGDTIDIE PWRAKAFPVI KDLVVDRGAL
     DRIIAAGGYI TAPTGSAPEA HSQLVRKADA DAAFESAACI GCGACVAACP NGSATLFLAA
     KVTHLSLLPQ GQPERMTRVV GMVDAHDAAG FGGCTNIGEC SAVCPKEIPL STIGRLNRDY
     LRATRERSGT PGT
//
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