ID   HIP1_ECTMO              Reviewed;          72 AA.
AC   P83341;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=High-potential iron-sulfur protein isozyme 1;
DE            Short=HiPIP 1;
OS   Ectothiorhodospira mobilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=195064;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CARBAMYLATION AT ALA-1, AND MASS SPECTROMETRY.
RX   PubMed=12203680; DOI=10.1002/jms.348;
RA   Van Driessche G.A.A., Vandenberghe I., Jacquemotte F., Devreese B.,
RA   Van Beeumen J.J.;
RT   "Mass spectrometric identification of in vivo carbamylation of the amino
RT   terminus of Ectothiorhodospira mobilis high-potential iron-sulfur protein,
RT   isozyme 1.";
RL   J. Mass Spectrom. 37:858-866(2002).
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. {ECO:0000250|UniProtKB:P38524}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P38524}.
CC   -!- MASS SPECTROMETRY: Mass=8104.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12203680};
CC   -!- MASS SPECTROMETRY: Mass=8147.2; Method=Electrospray; Note=With Ala-1
CC       carbamylated.; Evidence={ECO:0000269|PubMed:12203680};
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR   AlphaFoldDB; P83341; -.
DR   SMR; P83341; -.
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..72
FT                   /note="High-potential iron-sulfur protein isozyme 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000220418"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000305"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000305"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000305"
FT   BINDING         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-carbamoylalanine; partial"
FT                   /evidence="ECO:0000269|PubMed:12203680"
SQ   SEQUENCE   72 AA;  7758 MW;  BC682FF3BE157C1A CRC64;
     AEKLEESSAE AKALSYVHDA TTSGHDSYQE GQKCINCLLY TDPSQEEWGG CAVFPGKLVN
     ANGWCTAYVA RG