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Database: UniProt
Entry: A0A1Q4ZLN6_9ACTN
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ID   A0A1Q4ZLN6_9ACTN        Unreviewed;       258 AA.
AC   A0A1Q4ZLN6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Succinate dehydrogenase/fumarate reductase iron-sulfur subunit {ECO:0000313|EMBL:OKI47762.1};
GN   ORFNames=A6A29_01365 {ECO:0000313|EMBL:OKI47762.1};
OS   Streptomyces sp. TSRI0281.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI47762.1, ECO:0000313|Proteomes:UP000186952};
RN   [1] {ECO:0000313|EMBL:OKI47762.1, ECO:0000313|Proteomes:UP000186952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI47762.1,
RC   ECO:0000313|Proteomes:UP000186952};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI47762.1}.
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DR   EMBL; LWLE01000001; OKI47762.1; -; Genomic_DNA.
DR   RefSeq; WP_073718055.1; NZ_LWLE01000001.1.
DR   AlphaFoldDB; A0A1Q4ZLN6; -.
DR   STRING; 1718998.A6A29_01365; -.
DR   OrthoDB; 9804391at2; -.
DR   Proteomes; UP000186952; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186952}.
FT   DOMAIN          6..93
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   258 AA;  29066 MW;  525CCFF78038459A CRC64;
     MSGYEARFRV WRGDTEGGDL ADYTVEVNDG EVVLDIIHRI QATQAGDLAV RWNCKAGKCG
     SCSAEINGRP RLLCMTRMSV FSRQETITVT PLRAFPVVRD LVTDVTFNYT KAREVPAFVP
     PEGVKAGDYR MQQVDVDRSQ EFRKCIECFL CQDTCHVVRD HEENKAAFAG PRFLMRVAEL
     DMHPLDAAAE AGLDRKASAQ EEHGLGYCNI TKCCTEVCPE HIRITDNALI PLKERVVDRR
     YDPLVWLGNK IGRRREGG
//
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