ID NFUA_ENT38 Reviewed; 191 AA.
AC A4WFK2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=Ent638_3827;
OS Enterobacter sp. (strain 638).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
CC -!- FUNCTION: Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S
CC cluster, can transfer this cluster to apoproteins, and thereby
CC intervenes in the maturation of Fe/S proteins. Could also act as a
CC scaffold/chaperone for damaged Fe/S proteins. {ECO:0000255|HAMAP-
CC Rule:MF_01637}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01637};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is presumably
CC bound at the interface of two monomers. {ECO:0000255|HAMAP-
CC Rule:MF_01637};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01637}.
CC -!- SIMILARITY: Belongs to the NfuA family. {ECO:0000255|HAMAP-
CC Rule:MF_01637}.
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DR EMBL; CP000653; ABP62482.1; -; Genomic_DNA.
DR RefSeq; WP_015960787.1; NC_009436.1.
DR AlphaFoldDB; A4WFK2; -.
DR SMR; A4WFK2; -.
DR STRING; 399742.Ent638_3827; -.
DR KEGG; ent:Ent638_3827; -.
DR eggNOG; COG0316; Bacteria.
DR eggNOG; COG0694; Bacteria.
DR HOGENOM; CLU_094569_0_0_6; -.
DR OrthoDB; 9785450at2; -.
DR Proteomes; UP000000230; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0051604; P:protein maturation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR Gene3D; 2.60.300.12; HesB-like domain; 1.
DR HAMAP; MF_01637; Fe_S_biogen_NfuA; 1.
DR InterPro; IPR017726; Fe/S_biogenesis_protein_NfuA.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR NCBIfam; TIGR03341; YhgI_GntY; 1.
DR PANTHER; PTHR11178; IRON-SULFUR CLUSTER SCAFFOLD PROTEIN NFU-RELATED; 1.
DR PANTHER; PTHR11178:SF1; NFU1 IRON-SULFUR CLUSTER SCAFFOLD HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR Pfam; PF01106; NifU; 1.
DR SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR SUPFAM; SSF89360; HesB-like domain; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding.
FT CHAIN 1..191
FT /note="Fe/S biogenesis protein NfuA"
FT /id="PRO_1000069869"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
SQ SEQUENCE 191 AA; 20980 MW; F839C6508A40F90E CRC64;
MIRISDSAQA HFAKLLANQE EGTQIRVFVI NPGTPNAECG VSYCPPDAVE ASDTALKFEL
LTAYVDELSA PYLDDAEIDF VTDQLGSQLT LKAPNAKMRK VSDDAPLMER VEYLLQSQIN
PQLAGHGGRV TLMEITEDGL AILQFGGGCN GCSMVDVTLK EGIEKQMLNE FPELKGVRDL
TEHQRGEHSY Y
//
