ID A0A0J1JI32_9GAMM Unreviewed; 192 AA.
AC A0A0J1JI32;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ABT58_07435 {ECO:0000313|EMBL:KLV01592.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLV01592.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLV01592.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLV01592.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLV01592.1}.
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DR EMBL; LDOV01000011; KLV01592.1; -; Genomic_DNA.
DR RefSeq; WP_047873759.1; NZ_PYMF01000152.1.
DR AlphaFoldDB; A0A0J1JI32; -.
DR PATRIC; fig|754436.4.peg.1583; -.
DR OrthoDB; 9785450at2; -.
DR Proteomes; UP000036426; 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; 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 {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:UP000036426}.
FT DOMAIN 2..97
FT /note="FeS cluster biogenesis"
FT /evidence="ECO:0000259|Pfam:PF01521"
FT DOMAIN 111..172
FT /note="NIF system FeS cluster assembly NifU C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01106"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01637"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01637"
SQ SEQUENCE 192 AA; 20813 MW; 20D367CE12B4FDF0 CRC64;
MITISENAQQ HFGKLLAQQP EGTNIRVFVV NPGTQNAECG VSYCPPEAVE ATDTEIKFDL
FSAFVDELSL PFLDDAEIDF VTDKMGSQLT LKAPNAKVRK VSDDATLMER VDYVIQTQVN
PQLAGHGGNV SLAEITEDGV AILQFGGGCN GCSMVDVTLK EGIEKELLAQ FAGELTGVRD
ITEHARGEHS YY
//