ISCU_HAEIN
ID ISCU_HAEIN Reviewed; 126 AA.
AC Q57074; O05020;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU;
DE AltName: Full=Sulfur acceptor protein IscU;
GN Name=iscU; OrderedLocusNames=HI_0377;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SEQUENCE REVISION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR OF THE APO PROTEIN AND IN COMPLEX WITH ZN(2+), SUBUNIT,
RP AND COFACTOR.
RX PubMed=15522305; DOI=10.1016/j.jmb.2004.08.038;
RA Ramelot T.A., Cort J.R., Goldsmith-Fischman S., Kornhaber G.J., Xiao R.,
RA Shastry R., Acton T.B., Honig B., Montelione G.T., Kennedy M.A.;
RT "Solution NMR structure of the iron-sulfur cluster assembly protein U
RT (IscU) with zinc bound at the active site.";
RL J. Mol. Biol. 344:567-583(2004).
CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters.
CC Subsequently gives the nascent cluster to other proteins. It is likely
CC that Fe-S cluster coordination is flexible as the role of this complex
CC is to build and then hand off Fe-S clusters (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15522305};
CC Note=Binds 1 Zn(2+) ion; this is probably a substitute for Fe-S
CC centers. {ECO:0000269|PubMed:15522305};
CC -!- SUBUNIT: Forms a heterotetramer with IscS; each subunit of the IscS
CC dimer contacts an IscU monomer (By similarity). Upon overexpression can
CC be isolated a monomer, dimers and other oligomers. {ECO:0000250,
CC ECO:0000269|PubMed:15522305}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; L42023; AAC22034.1; -; Genomic_DNA.
DR RefSeq; NP_438538.2; NC_000907.1.
DR RefSeq; WP_005654861.1; NC_000907.1.
DR PDB; 1Q48; NMR; -; A=1-126.
DR PDB; 1R9P; NMR; -; A=1-126.
DR PDBsum; 1Q48; -.
DR PDBsum; 1R9P; -.
DR AlphaFoldDB; Q57074; -.
DR BMRB; Q57074; -.
DR SMR; Q57074; -.
DR STRING; 71421.HI_0377; -.
DR EnsemblBacteria; AAC22034; AAC22034; HI_0377.
DR KEGG; hin:HI_0377; -.
DR PATRIC; fig|71421.8.peg.395; -.
DR eggNOG; COG0822; Bacteria.
DR HOGENOM; CLU_079283_5_0_6; -.
DR OMA; YKNPRNY; -.
DR PhylomeDB; Q57074; -.
DR EvolutionaryTrace; Q57074; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR01999; iscU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..126
FT /note="Iron-sulfur cluster assembly scaffold protein IscU"
FT /id="PRO_0000166187"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1Q48"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1Q48"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1Q48"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1Q48"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1Q48"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1Q48"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:1Q48"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1Q48"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:1Q48"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1Q48"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1Q48"
FT HELIX 105..123
FT /evidence="ECO:0007829|PDB:1Q48"
SQ SEQUENCE 126 AA; 13399 MW; 9918E1334646E67B CRC64;
MAYSEKVIDH YENPRNVGSL DKKDSNVGTG MVGAPACGDV MQLQIKVDDN GIIEDAKFKT
YGCGSAIASS SLITEWVKGK SLEEAGAIKN SQIAEELELP PVKVHCSILA EDAIKAAIAD
YKAKQG
