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Database: UniProt
Entry: D1AZG4_SULD5
LinkDB: D1AZG4_SULD5
Original site: D1AZG4_SULD5 
ID   D1AZG4_SULD5            Unreviewed;       260 AA.
AC   D1AZG4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Fumarate reductase cytochrome b subunit {ECO:0000256|PIRNR:PIRNR000177};
GN   OrderedLocusNames=Sdel_0394 {ECO:0000313|EMBL:ACZ11431.1};
OS   Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurospirillaceae; Sulfurospirillum.
OX   NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ11431.1, ECO:0000313|Proteomes:UP000002222};
RN   [1] {ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Munk A.C., Lu M., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Aumann P., Schneider S., Lang E.,
RA   Spring S., Klenk H.P., Eisen J.A.;
RT   "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ11431.1, ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RX   PubMed=21304697; DOI=10.4056/sigs.671209;
RA   Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., Goodwin L.,
RA   Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Detter J.C., Han C., Rohde M., Lang E., Spring S., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT   (5175).";
RL   Stand. Genomic Sci. 2:149-157(2010).
CC   -!- FUNCTION: The fumarate reductase enzyme complex is required for
CC       fumarate respiration. This subunit anchors the complex in the membrane
CC       and binds a diheme cytochrome b. {ECO:0000256|PIRNR:PIRNR000177}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR000177}.
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DR   EMBL; CP001816; ACZ11431.1; -; Genomic_DNA.
DR   RefSeq; WP_012856197.1; NC_013512.1.
DR   AlphaFoldDB; D1AZG4; -.
DR   STRING; 525898.Sdel_0394; -.
DR   KEGG; sdl:Sdel_0394; -.
DR   eggNOG; ENOG502ZBTX; Bacteria.
DR   HOGENOM; CLU_075821_0_0_7; -.
DR   OrthoDB; 5345350at2; -.
DR   Proteomes; UP000002222; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd00581; QFR_TypeB_TM; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR004224; Fum_red_B_TM.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000177; Fumar_rd_cyt_b; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR000177};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000177};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000177};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000177};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000177};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000177};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002222};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR000177};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000177}.
FT   TRANSMEM        26..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         42
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="bD"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
FT   BINDING         91
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="bD"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
FT   BINDING         141
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="bD"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
FT   BINDING         180
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="bD"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
SQ   SEQUENCE   260 AA;  29919 MW;  9A71EBA9D41ECE78 CRC64;
     MNDLLEGFLG TSIEGKKSRV PAKLDYIQSA TGLFLGLFMW GHMFFVSTIL ISKDFMHTIT
     KMFEGSMFFS EPQPWVVSAI VLFVFAIFIV HAMLGMRKLP ITFRQYQAYK THMGMMKHDD
     TTMWFTQAFT GFAMFFLGSA HLLMMAVKAD EIGPYGSSER MYADVMWPFY LLLLLAVEFH
     GGIGLYRLCV KWGWFEGENV KESRKKLKKV KWAVTTFFLA LGLLTLAAYV KYGYEYSNGH
     VDEFKPTAQL ELRIDQKVRA
//
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