HIP2_RHOTE
ID HIP2_RHOTE Reviewed; 62 AA.
AC P33678;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=High-potential iron-sulfur protein;
DE Short=HiPIP;
GN Name=hip;
OS Rhodocyclus tenuis (Rhodospirillum tenue).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Rhodocyclus.
OX NCBI_TaxID=1066;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=2761;
RX PubMed=4004266; DOI=10.1016/0003-9861(85)90815-x;
RA Tedro S.M., Meyer T.E., Kamen M.D.;
RT "The amino acid sequence of a high-redox-potential ferredoxin from the
RT purple phototrophic bacterium, Rhodospirillum tenue strain 2761.";
RL Arch. Biochem. Biophys. 239:94-101(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S),
RP AND SEQUENCE REVISION.
RC STRAIN=2761;
RX PubMed=1453470; DOI=10.1016/0022-2836(92)90849-f;
RA Rayment I., Wesenberg G., Meyer T.E., Cusanovich M.A., Holden H.M.;
RT "Three-dimensional structure of the high-potential iron-sulfur protein
RT isolated from the purple phototrophic bacterium Rhodocyclus tenuis
RT determined and refined at 1.5-A resolution.";
RL J. Mol. Biol. 228:672-686(1992).
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 +330 mV.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR PIR; A55789; A55789.
DR PDB; 1ISU; X-ray; 1.50 A; A/B=1-62.
DR PDBsum; 1ISU; -.
DR AlphaFoldDB; P33678; -.
DR SMR; P33678; -.
DR EvolutionaryTrace; P33678; -.
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..62
FT /note="High-potential iron-sulfur protein"
FT /id="PRO_0000220428"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1453470"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1453470"
FT BINDING 40
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1453470"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:1453470"
FT CONFLICT 30
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:1ISU"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1ISU"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1ISU"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1ISU"
SQ SEQUENCE 62 AA; 6296 MW; 76360061AB43F88D CRC64;
GTNAAMRKAF NYQDTAKNGK KCSGCAQFVP GASPTAAGGC KVIPGDNQIA PGGYCDAFIV
KK
