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Database: UniProt
Entry: G4CU26_9ACTN
LinkDB: G4CU26_9ACTN
Original site: G4CU26_9ACTN 
ID   G4CU26_9ACTN            Unreviewed;       257 AA.
AC   G4CU26;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   07-NOV-2018, entry version 32.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN   Name=frdB {ECO:0000313|EMBL:EGY79267.1};
GN   ORFNames=HMPREF9153_0032 {ECO:0000313|EMBL:EGY79267.1};
OS   Cutibacterium avidum ATCC 25577.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=997355 {ECO:0000313|EMBL:EGY79267.1, ECO:0000313|Proteomes:UP000005332};
RN   [1] {ECO:0000313|EMBL:EGY79267.1, ECO:0000313|Proteomes:UP000005332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25577 {ECO:0000313|EMBL:EGY79267.1,
RC   ECO:0000313|Proteomes:UP000005332};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC       {ECO:0000256|RuleBase:RU361237}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family.
CC       {ECO:0000256|RuleBase:RU361237}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGY79267.1}.
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DR   EMBL; AGBA01000001; EGY79267.1; -; Genomic_DNA.
DR   RefSeq; WP_004808573.1; NZ_JH165054.1.
DR   EnsemblBacteria; EGY79267; EGY79267; HMPREF9153_0032.
DR   PATRIC; fig|997355.3.peg.34; -.
DR   Proteomes; UP000005332; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.10.20.30; -; 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; IPR017900; 4Fe4S_Fe_S_CS.
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   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|RuleBase:RU361237};
KW   3Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   4Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005332};
KW   Iron {ECO:0000256|RuleBase:RU361237};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU361237};
KW   Metal-binding {ECO:0000256|RuleBase:RU361237};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005332}.
FT   DOMAIN        1    108       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
FT   DOMAIN      155    184       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      207    240       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
SQ   SEQUENCE   257 AA;  27577 MW;  38882D000654FB66 CRC64;
     MKINLRIWRQ RNTQDQGRLV EYTLDGVSGD MSFLEMLDML NENLTAQGEE PVAFDSDCRE
     GICGQCGVVI NGVPHGGMGV AQPVRTTTCQ LHMRSFADGS TITIEPWKSG AFPILRDLIV
     DRSALDRVIQ AGGYISVNTG AAPDAHAVQV NKKRSDRSFD AATCIGCGAC VAACPNGSSM
     LFTSAKITHL AMLPQGQPER MRRVKAMAAQ NDAEGFGGCT NIGECASVCP KGIPLESISQ
     LNRDLIASLF KHDGKDD
//
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