HIP1_HALHA
ID HIP1_HALHA Reviewed; 71 AA.
AC P04168;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=High-potential iron-sulfur protein isozyme 1 {ECO:0000303|PubMed:4037807};
DE Short=HiPIP 1 {ECO:0000303|PubMed:4037807};
DE AltName: Full=High-redox-potential ferredoxin 1 {ECO:0000305};
GN Name=hip1;
OS Halorhodospira halophila (Ectothiorhodospira halophila).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1053;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4037807; DOI=10.1016/0003-9861(85)90592-2;
RA Tedro S.M., Meyer T.E., Kamen M.D.;
RT "Amino acid sequence of high-redox-potential ferredoxin (HiPIP) isozymes
RT from the extremely halophilic purple phototrophic bacterium,
RT Ectothiorhodospira halophila.";
RL Arch. Biochem. Biophys. 241:656-664(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S),
RP AND SEQUENCE REVISION TO 19-23.
RC STRAIN=BN9626;
RX PubMed=1917989; DOI=10.2210/pdb2hip/pdb;
RA Breiter D.R., Meyer T.E., Rayment I., Holden H.M.;
RT "The molecular structure of the high potential iron-sulfur protein isolated
RT from Ectothiorhodospira halophila determined at 2.5-A resolution.";
RL J. Biol. Chem. 266:18660-18667(1991).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=7957186; DOI=10.1111/j.1432-1033.1994.00703.x;
RA Bertini I., Felli I.C., Kastrau D.H., Luchinat C., Piccioli M.,
RA Viezzoli M.S.;
RT "Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance
RT spectra of the reduced recombinant high-potential iron-sulfur protein I
RT from Ectothiorhodospira halophila.";
RL Eur. J. Biochem. 225:703-714(1994).
RN [4]
RP STRUCTURE BY NMR IN COMPLEX WITH IRON-SULFUR (4FE-4S).
RX PubMed=7957187; DOI=10.1111/j.1432-1033.1994.00715.x;
RA Banci L., Bertini I., Eltis L.D., Felli I.C., Kastrau D.H.W., Luchinat C.,
RA Piccioli M., Pierattelli R., Smith M.;
RT "The three-dimensional structure in solution of the paramagnetic high-
RT potential iron-sulfur protein I from Ectothiorhodospira halophila through
RT nuclear magnetic resonance.";
RL Eur. J. Biochem. 225:715-725(1994).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8917441; DOI=10.1111/j.1432-1033.1996.00440.x;
RA Bertini I., Couture M.M.J., Donaire A., Eltis L.D., Felli I.C.,
RA Luchinat C., Piccioli M., Rosati A.;
RT "The solution structure refinement of the paramagnetic reduced high-
RT potential iron-sulfur protein I from Ectothiorhodospira halophila by using
RT stable isotope labeling and nuclear relaxation.";
RL Eur. J. Biochem. 241:440-452(1996).
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.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +120 mV.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- MISCELLANEOUS: In E.halophila, two HiPIP isozymes are found.
CC -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR PIR; S48703; IHER1.
DR PDB; 1PIH; NMR; -; A=1-71.
DR PDB; 1PIJ; NMR; -; A=1-71.
DR PDB; 2HIP; X-ray; 2.50 A; A/B=1-71.
DR PDBsum; 1PIH; -.
DR PDBsum; 1PIJ; -.
DR PDBsum; 2HIP; -.
DR AlphaFoldDB; P04168; -.
DR BMRB; P04168; -.
DR SMR; P04168; -.
DR EvolutionaryTrace; P04168; -.
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..71
FT /note="High-potential iron-sulfur protein isozyme 1"
FT /id="PRO_0000220416"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1917989,
FT ECO:0000269|PubMed:7957187"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1917989,
FT ECO:0000269|PubMed:7957187"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1917989,
FT ECO:0000269|PubMed:7957187"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1917989,
FT ECO:0000269|PubMed:7957187"
FT CONFLICT 19..23
FT /note="ASGHP -> PSHG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2HIP"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2HIP"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2HIP"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2HIP"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2HIP"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2HIP"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2HIP"
SQ SEQUENCE 71 AA; 7837 MW; E65C3F2C39A22C24 CRC64;
EPRAEDGHAH DYVNEAADAS GHPRYQEGQL CENCAFWGEA VQDGWGRCTH PDFDEVLVKA
EGWCSVYAPA S
