ID   HIP2_HALHA              Reviewed;          76 AA.
AC   P04169;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=High-potential iron-sulfur protein isozyme 2 {ECO:0000303|PubMed:4037807};
DE            Short=HiPIP 2 {ECO:0000303|PubMed:4037807};
DE   AltName: Full=High-redox-potential ferredoxin 2 {ECO:0000305};
GN   Name=hip2;
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).
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 +50 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}.
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   PIR; A00271; IHER2.
DR   AlphaFoldDB; P04169; -.
DR   SMR; P04169; -.
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   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Transport.
FT   CHAIN           1..76
FT                   /note="High-potential iron-sulfur protein isozyme 2"
FT                   /id="PRO_0000220417"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   BINDING         41
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   BINDING         70
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
SQ   SEQUENCE   76 AA;  8560 MW;  12D1524EB0BAF7AC CRC64;
     GLPDGVEDLP KAEDDHAHDY VNDAADTDHA RFQEGQLCEN CQFWVDYVNG WGYCQHPDFT
     DVLVRGEGWC SVYAPA