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Database: UniProt
Entry: R4QKG9_HELPX
LinkDB: R4QKG9_HELPX
Original site: R4QKG9_HELPX 
ID   R4QKG9_HELPX            Unreviewed;       245 AA.
AC   R4QKG9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Fumarate reductase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN   Name=frdB {ECO:0000313|EMBL:AGL70442.1};
GN   ORFNames=K750_07600 {ECO:0000313|EMBL:AGL70442.1};
OS   Helicobacter pylori UM037.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1321939 {ECO:0000313|EMBL:AGL70442.1, ECO:0000313|Proteomes:UP000013898};
RN   [1] {ECO:0000313|EMBL:AGL70442.1, ECO:0000313|Proteomes:UP000013898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UM037 {ECO:0000313|EMBL:AGL70442.1,
RC   ECO:0000313|Proteomes:UP000013898};
RA   Khosravi Y., Rehvathy V., Amoyo A., Seow S., Ong J., Susana W., Primo B.,
RA   Meredith A., Siddarth S., Pettersson S., Loke M., Goh K., Vadivelu J.;
RT   "Draft Genome Sequences of Helicobacter pylori Strain UM037 and UM066 using
RT   PacBio Sequencing Platform.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a menaquinone + succinate = a menaquinol + fumarate;
CC         Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539,
CC         ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031; EC=1.3.5.1;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
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 reductase
CC       iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433,
CC       ECO:0000256|RuleBase:RU361237}.
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DR   EMBL; CP005492; AGL70442.1; -; Genomic_DNA.
DR   RefSeq; WP_001282432.1; NZ_AUSI01000006.1.
DR   AlphaFoldDB; R4QKG9; -.
DR   KEGG; hpyi:K750_07600; -.
DR   PATRIC; fig|1321939.6.peg.1583; -.
DR   HOGENOM; CLU_044838_3_3_7; -.
DR   Proteomes; UP000013898; Chromosome.
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:0102040; F:fumarate reductase (menaquinone); IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; 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; 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   NCBIfam; TIGR00384; dhsB; 1.
DR   PANTHER; PTHR11921:SF36; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 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.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU361237};
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU361237};
KW   4Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361237};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361237};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          17..98
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          145..174
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   245 AA;  27611 MW;  8FE0C002CFF5D949 CRC64;
     MSDNERTIVV RVLKFDPQSA VSKPHFKEYQ LKETPSMTLF IALNLIREHQ DPDLSFDFVC
     RAGICGSCAM MVNGRPRLAC KTLTSSFESG VITLMPMPSF TLIKDLSVNT GDWFLDMTKR
     VESWAHSKEE VDITKPEKRI EPDEAQEVFE LDRCIECGCC IASCGTKLMR PNFIGAAGMN
     RAMRFMIDSH DERSDDDFYE LVGDDDGVFG CMSLIACHDT CPKELPLQSS IATLRNRMLK
     VGKSR
//
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