GenomeNet

Database: UniProt
Entry: A0A0Q0GJD1_9GAMM
LinkDB: A0A0Q0GJD1_9GAMM
Original site: A0A0Q0GJD1_9GAMM 
ID   A0A0Q0GJD1_9GAMM        Unreviewed;       245 AA.
AC   A0A0Q0GJD1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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:KPZ72333.1};
GN   ORFNames=AN944_01111 {ECO:0000313|EMBL:KPZ72333.1};
OS   Shewanella sp. P1-14-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ72333.1, ECO:0000313|Proteomes:UP000050414};
RN   [1] {ECO:0000313|EMBL:KPZ72333.1, ECO:0000313|Proteomes:UP000050414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ72333.1,
RC   ECO:0000313|Proteomes:UP000050414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000030};
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}.
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:KPZ72333.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LKTL01000005; KPZ72333.1; -; Genomic_DNA.
DR   RefSeq; WP_055023586.1; NZ_LKTL01000005.1.
DR   AlphaFoldDB; A0A0Q0GJD1; -.
DR   PATRIC; fig|1723761.3.peg.1146; -.
DR   Proteomes; UP000050414; 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: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: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: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; 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|RuleBase:RU361237};
KW   4Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   Iron {ECO:0000256|RuleBase:RU361237};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU361237};
KW   Metal-binding {ECO:0000256|RuleBase:RU361237};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050414};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT   DOMAIN          21..97
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          144..174
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   245 AA;  27424 MW;  7A5469E0ACF1714C CRC64;
     MSAPRTISFD IFRYDPQDPN DKPKMVTYEI TEAPGMTVFI ALNLLREQQD PSLQFDFVCR
     AGICGSCAMV INGKPTLACR TLTANFPDGK IKLMPLPGFE LIGDLSVNTG KFMRELAERL
     QLWLQPDSND IDIHRLENPM DPAEAAKLYE LERCVECGVC VSACATKQMK DTFVGAVGMM
     KIARFEMDSR DTRTAEDFYH VIGNQDGVFG CMTLLGCQDA CPKDLPHMQQ IAYLRRKMAQ
     TIVSC
//
DBGET integrated database retrieval system