ID   HIP_RHOFE               Reviewed;          75 AA.
AC   P80882;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=High-potential iron-sulfur protein;
DE            Short=HiPIP;
GN   Name=hip;
OS   Rhodoferax fermentans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=28066;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   STRAIN=JMC 7819;
RX   PubMed=9119002; DOI=10.1111/j.1432-1033.1997.00371.x;
RA   van Driessche G., Ciurli S., Hochkoeppler A., van Beeumen J.J.;
RT   "The primary structure of Rhodoferax fermentans high-potential iron-sulfur
RT   protein, an electron donor to the photosynthetic reaction center.";
RL   Eur. J. Biochem. 244:371-377(1997).
RN   [2]
RP   FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=7574702; DOI=10.1006/abbi.1995.1469;
RA   Hochkoeppler A., Kofod P., Ferro G., Ciurli S.;
RT   "Isolation, characterization, and functional role of the high-potential
RT   iron-sulfur protein (HiPIP) from Rhodoferax fermentans.";
RL   Arch. Biochem. Biophys. 322:313-318(1995).
RN   [3]
RP   FUNCTION.
RC   STRAIN=JMC 7819;
RX   DOI=10.1016/0005-2728(94)00189-C;
RA   Hochkoeppler A., Moschettini G., Zannoni D.;
RT   "The electron transport system of the facultative phototroph Rhodoferax
RT   fermentans. I. A functional, thermodynamic and spectroscopic study of the
RT   respiratory chain of dark- and light-grown cells.";
RL   Biochim. Biophys. Acta 1229:73-80(1995).
RN   [4]
RP   FUNCTION.
RX   PubMed=8001683; DOI=10.1016/0014-5793(94)01334-w;
RA   Hochkoeppler A., Ciurli S., Venturoli G., Zannoni D.;
RT   "The high potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans
RT   is competent in photosynthetic electron transfer.";
RL   FEBS Lett. 357:70-74(1995).
RN   [5]
RP   FUNCTION.
RX   PubMed=7498498; DOI=10.1016/0014-5793(95)01188-k;
RA   Hochkoeppler A., Kofod P., Zannoni D.;
RT   "HiPiP oxido-reductase activity in membranes from aerobically grown cells
RT   of the facultative phototroph Rhodoferax fermentans.";
RL   FEBS Lett. 375:197-200(1995).
RN   [6]
RP   FUNCTION.
RX   PubMed=8692932; DOI=10.1073/pnas.93.14.6998;
RA   Hochkoeppler A., Zannoni D., Ciurli S., Meyer T.E., Cusanovich M.A.,
RA   Tollin G.;
RT   "Kinetics of photo-induced electron transfer from high-potential iron-
RT   sulfur protein to the photosynthetic reaction center of the purple
RT   phototroph Rhodoferax fermentans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:6998-7002(1996).
RN   [7]
RP   FUNCTION.
RX   PubMed=10076014; DOI=10.1016/s0005-2728(98)00173-x;
RA   Bonora P., Principi I., Monti B., Ciurli S., Zannoni D., Hochkoeppler A.;
RT   "On the role of high-potential iron-sulfur proteins and cytochromes in the
RT   respiratory chain of two facultative phototrophs.";
RL   Biochim. Biophys. Acta 1410:51-60(1999).
RN   [8]
RP   STRUCTURE BY NMR, AND METAL-BINDING.
RX   PubMed=8612609; DOI=10.1111/j.1432-1033.1996.00405.x;
RA   Ciurli S., Cremonini M.A., Kofod P., Luchinat C.;
RT   "1H NMR of high-potential iron-sulfur protein from the purple non-
RT   sulfurbacterium Rhodoferax fermentans.";
RL   Eur. J. Biochem. 236:405-411(1996).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP   (4FE-4S).
RX   PubMed=12925788; DOI=10.1107/s0907444903014604;
RA   Gonzalez A., Benini S., Ciurli S.;
RT   "Structure of Rhodoferax fermentans high-potential iron-sulfur protein
RT   solved by MAD.";
RL   Acta Crystallogr. D 59:1582-1588(2003).
CC   -!- FUNCTION: Specific class of high-redox-potential 4Fe-4S ferredoxins.
CC       Functions in anaerobic electron transport in most purple and in some
CC       other photosynthetic bacteria and in at least one genus (Paracoccus) of
CC       halophilic, denitrifying bacteria. Competent in photosynthetic electron
CC       transfer to oxidized cytochrome bc1 complex via the membrane-bound c-
CC       type tetraheme. {ECO:0000255|PROSITE-ProRule:PRU00705,
CC       ECO:0000269|PubMed:10076014, ECO:0000269|PubMed:7498498,
CC       ECO:0000269|PubMed:7574702, ECO:0000269|PubMed:8001683,
CC       ECO:0000269|PubMed:8692932, ECO:0000269|Ref.3}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is 351 +/-16 mV. {ECO:0000269|PubMed:7574702};
CC   -!- SUBUNIT: Homodimer (By similarity). Monomer at different ionic
CC       strengths (PubMed:7574702). {ECO:0000250, ECO:0000269|PubMed:7574702}.
CC   -!- MASS SPECTROMETRY: Mass=7849.64; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9119002};
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR   PDB; 1HLQ; X-ray; 1.45 A; A/B/C=1-75.
DR   PDBsum; 1HLQ; -.
DR   AlphaFoldDB; P80882; -.
DR   SMR; P80882; -.
DR   STRING; 28066.RF819_00185; -.
DR   EvolutionaryTrace; P80882; -.
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:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR   Gene3D; 4.10.490.10; -; 1.
DR   InterPro; IPR000170; High_potential_FeS_prot.
DR   InterPro; IPR036369; HIPIP_sf.
DR   Pfam; PF01355; HIPIP; 1.
DR   SUPFAM; SSF57652; SSF57652; 1.
DR   PROSITE; PS51373; HIPIP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Transport.
FT   CHAIN           1..75
FT                   /note="High-potential iron-sulfur protein"
FT                   /id="PRO_0000220424"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:12925788"
FT   BINDING         41
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:12925788"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:12925788"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:12925788"
FT   HELIX           10..14
FT                   /evidence="ECO:0007829|PDB:1HLQ"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:1HLQ"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:1HLQ"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:1HLQ"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:1HLQ"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1HLQ"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:1HLQ"
SQ   SEQUENCE   75 AA;  7849 MW;  9FE6C86E662A72D3 CRC64;
     AAPLVAETDA NAKSLGYVAD TTKADKTKYP KHTKDQSCST CALYQGKTAP QGACPLFAGK
     EVVAKGWCSA WAKKA