HIP_ALLVD
ID HIP_ALLVD Reviewed; 122 AA.
AC P00260; D3RMQ3; P96753; Q9R4K3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=High-potential iron-sulfur protein;
DE Short=HiPIP;
DE Flags: Precursor;
GN Name=hip; OrderedLocusNames=Alvin_2274;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9177478; DOI=10.1016/s0167-4781(97)00033-x;
RA Bruser T., Truper H.G., Dahl C.;
RT "Cloning and sequencing of the gene encoding the high potential iron-sulfur
RT protein (HiPIP) from the purple sulfur bacterium Chromatium vinosum.";
RL Biochim. Biophys. Acta 1352:18-22(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [3]
RP PROTEIN SEQUENCE OF 38-122.
RX PubMed=4745771; DOI=10.1016/s0021-9258(19)43292-4;
RA Dus K., Tedro S., Bartsch R.G.;
RT "The complete amino acid sequence of Chromatium high potential iron sulfur
RT protein.";
RL J. Biol. Chem. 248:7318-7331(1973).
RN [4]
RP SEQUENCE REVISION TO 48; 82 AND 111.
RX PubMed=7451471; DOI=10.1016/s0021-9258(19)70036-2;
RA Tedro S.M., Meyer T.E., Bartsch R.G., Kamen M.D.;
RT "Primary structures of high potential, four-iron-sulfur ferredoxins from
RT the purple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and
RT Chromatium gracile.";
RL J. Biol. Chem. 256:731-735(1981).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S).
RX PubMed=4855287; DOI=10.1016/s0021-9258(19)42505-2;
RA Carter C.W. Jr., Kraut J., Freer S.T., Xuong N.H., Alden R.A.,
RA Bartsch R.G.;
RT "2-A crystal structure of oxidized Chromatium high potential iron
RT protein.";
RL J. Biol. Chem. 249:4212-4225(1974).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=1734968; DOI=10.1021/bi00119a037;
RA Nettesheim D.G., Harder S.R., Feinberg B.A., Otvos J.D.;
RT "Sequential resonance assignments of oxidized high-potential iron-sulfur
RT protein from Chromatium vinosum.";
RL Biochemistry 31:1234-1244(1992).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=1610810; DOI=10.1021/bi00139a029;
RA Gaillard J., Albrand J.-P., Moulis J.-M., Wemmer D.E.;
RT "Sequence-specific assignments of the 1H nuclear magnetic resonance spectra
RT of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum.";
RL Biochemistry 31:5632-5639(1992).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=7819198; DOI=10.1021/bi00001a025;
RA Banci L., Bertini I., Dikiy A., Kastrau D.H.W., Luchinat C.,
RA Sompornpisut P.;
RT "The three-dimensional solution structure of the reduced high-potential
RT iron-sulfur protein from Chromatium vinosum through NMR.";
RL Biochemistry 34:206-219(1995).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=7632685; DOI=10.1021/bi00031a005;
RA Bertini I., Dikiy A., Kastrau D.H., Luchinat C., Sompornpisut P.;
RT "Three-dimensional solution structure of the oxidized high potential iron-
RT sulfur protein from Chromatium vinosum through NMR. Comparative analysis
RT with the solution structure of the reduced species.";
RL Biochemistry 34:9851-9858(1995).
RN [10]
RP STRUCTURE BY NMR OF MUTANT SER-114.
RX PubMed=8639555; DOI=10.1021/bi9528513;
RA Bentrop D., Bertini I., Cappozi F., Dikiy A., Eltis L., Luchinat C.;
RT "Three-dimensional structure of the reduced C77S mutant of the Chromatium
RT vinosum high-potential iron-sulfur protein through nuclear magnetic
RT resonance: comparison with the solution structure of the wild-type
RT protein.";
RL Biochemistry 35:5928-5936(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (0.93 ANGSTROMS).
RX PubMed=10531472; DOI=10.1107/s0907444999009129;
RA Parisini E., Capozzi F., Lubini P., Lamzin V., Luchinat C., Sheldrick G.M.;
RT "Ab initio solution and refinement of two high-potential iron protein
RT structures at atomic resolution.";
RL Acta Crystallogr. D 55:1773-1784(1999).
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 +360 mV.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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 EMBL; U81381; AAB48829.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63191.1; -; Genomic_DNA.
DR RefSeq; WP_012971463.1; NC_013851.1.
DR PDB; 1B0Y; X-ray; 0.93 A; A=38-122.
DR PDB; 1CKU; X-ray; 1.20 A; A/B=38-122.
DR PDB; 1HIP; X-ray; 2.00 A; A=38-122.
DR PDB; 1HRQ; NMR; -; A=38-122.
DR PDB; 1HRR; NMR; -; A=38-122.
DR PDB; 1JS2; X-ray; 1.90 A; A/B/C/D=38-122.
DR PDB; 1NEH; NMR; -; A=38-122.
DR PDB; 1NOE; NMR; -; A=37-122.
DR PDBsum; 1B0Y; -.
DR PDBsum; 1CKU; -.
DR PDBsum; 1HIP; -.
DR PDBsum; 1HRQ; -.
DR PDBsum; 1HRR; -.
DR PDBsum; 1JS2; -.
DR PDBsum; 1NEH; -.
DR PDBsum; 1NOE; -.
DR AlphaFoldDB; P00260; -.
DR BMRB; P00260; -.
DR SMR; P00260; -.
DR STRING; 572477.Alvin_2274; -.
DR EnsemblBacteria; ADC63191; ADC63191; Alvin_2274.
DR KEGG; alv:Alvin_2274; -.
DR eggNOG; ENOG50330XW; Bacteria.
DR HOGENOM; CLU_147871_0_0_6; -.
DR OMA; VNAKGWC; -.
DR OrthoDB; 2004268at2; -.
DR EvolutionaryTrace; P00260; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 InterPro; IPR006311; TAT_signal.
DR Pfam; PF01355; HIPIP; 1.
DR SUPFAM; SSF57652; SSF57652; 1.
DR PROSITE; PS51373; HIPIP; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:4745771"
FT CHAIN 38..122
FT /note="High-potential iron-sulfur protein"
FT /id="PRO_0000013438"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:4855287"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:4855287"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:4855287"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:4855287"
FT CONFLICT 111
FT /note="N -> D (in Ref. 4)"
FT /evidence="ECO:0000305"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1B0Y"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1B0Y"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1B0Y"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1B0Y"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1JS2"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1B0Y"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1B0Y"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1JS2"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1B0Y"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1B0Y"
SQ SEQUENCE 122 AA; 12762 MW; ACBBAFC917F32A09 CRC64;
MSDKPISKSR RDAVKVMLGT AAAIPMINLV GFGTARASAP ANAVAADDAT AIALKYNQDA
TKSERVAAAR PGLPPEEQHC ANCQFMQADA AGATDEWKGC QLFPGKLINV NGWCASWTLK
AG
