ID A0A1I1EUJ3_9GAMM Unreviewed; 202 AA.
AC A0A1I1EUJ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 25.
DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000256|HAMAP-Rule:MF_01637};
GN Name=nfuA {ECO:0000256|HAMAP-Rule:MF_01637};
GN ORFNames=SAMN05660443_0769 {ECO:0000313|EMBL:SFB89198.1};
OS Marinospirillum celere.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Oceanospirillaceae; Marinospirillum.
OX NCBI_TaxID=1122252 {ECO:0000313|EMBL:SFB89198.1, ECO:0000313|Proteomes:UP000199058};
RN [1] {ECO:0000313|EMBL:SFB89198.1, ECO:0000313|Proteomes:UP000199058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18438 {ECO:0000313|EMBL:SFB89198.1,
RC ECO:0000313|Proteomes:UP000199058};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_01637}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01637};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01637}.
CC -!- SIMILARITY: Belongs to the NfuA family. {ECO:0000256|HAMAP-
CC Rule:MF_01637}.
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; FOLH01000001; SFB89198.1; -; Genomic_DNA.
DR RefSeq; WP_091959380.1; NZ_FOLH01000001.1.
DR AlphaFoldDB; A0A1I1EUJ3; -.
DR STRING; 1122252.SAMN05660443_0769; -.
DR OrthoDB; 9785450at2; -.
DR Proteomes; UP000199058; Unassembled WGS sequence.
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; IPR000361; ATAP_core_dom.
DR InterPro; IPR017726; Fe/S_biogenesis_protein_NfuA.
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:SF51; FE_S BIOGENESIS PROTEIN NFUA; 1.
DR PANTHER; PTHR11178; IRON-SULFUR CLUSTER SCAFFOLD PROTEIN NFU-RELATED; 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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01637};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01637};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01637};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01637}; Reference proteome {ECO:0000313|Proteomes:UP000199058}.
FT DOMAIN 11..107
FT /note="Core"
FT /evidence="ECO:0000259|Pfam:PF01521"
FT DOMAIN 121..186
FT /note="NIF system FeS cluster assembly NifU C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01106"
FT BINDING 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01637"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01637"
SQ SEQUENCE 202 AA; 22132 MW; 381A103EA97A73EE CRC64;
MSDVEAPSKP LEITESAENY LAELLAKQEV ADMGVRVFIT QPGTPYAETC LAYCRPGEEE
ATDQLVELEK IKVFLEKNSV PFLDEAVVDF NPDRMGGQLT IKAPNAKMPK VSKDSPLGDQ
INYILYSDIN PGLAAHGGEI KLIELTDDNV AVLQFGGGCQ GCSAVDLTLK DGVERTLLER
LPELKGIRDV TDHTVKENAY YK
//