ID N9TWE5_9GAMM Unreviewed; 135 AA.
AC N9TWE5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Ferredoxin-type protein NapF {ECO:0000256|HAMAP-Rule:MF_02201};
GN Name=napF {ECO:0000256|HAMAP-Rule:MF_02201};
GN ORFNames=G114_18646 {ECO:0000313|EMBL:ENY70380.1};
OS Aeromonas diversa CDC 2478-85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY70380.1, ECO:0000313|Proteomes:UP000023775};
RN [1] {ECO:0000313|EMBL:ENY70380.1, ECO:0000313|Proteomes:UP000023775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2478-85 {ECO:0000313|EMBL:ENY70380.1,
RC ECO:0000313|Proteomes:UP000023775};
RX PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA Fuste M.C.;
RT "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL Genome Announc. 1:S69-S82(2013).
CC -!- FUNCTION: Could be involved in the maturation of NapA, the catalytic
CC subunit of the periplasmic nitrate reductase, before its export into
CC the periplasm. {ECO:0000256|HAMAP-Rule:MF_02201}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02201};
CC -!- SUBUNIT: Interacts with the cytoplasmic NapA precursor.
CC {ECO:0000256|HAMAP-Rule:MF_02201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02201}.
CC -!- SIMILARITY: Belongs to the NapF family. {ECO:0000256|HAMAP-
CC Rule:MF_02201}.
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:ENY70380.1}.
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DR EMBL; APVG01000083; ENY70380.1; -; Genomic_DNA.
DR AlphaFoldDB; N9TWE5; -.
DR PATRIC; fig|1268237.3.peg.3651; -.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR Proteomes; UP000023775; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd10564; NapF_like; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR HAMAP; MF_02201; NapF; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004496; NapF.
DR NCBIfam; TIGR00402; napF; 1.
DR PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR PANTHER; PTHR43687:SF1; L-ASPARTATE SEMIALDEHYDE SULFURTRANSFERASE IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_02201};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02201};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02201};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_02201};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02201};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_02201}.
FT DOMAIN 1..24
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 25..56
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 99..128
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 4
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 7
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 36
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
SQ SEQUENCE 135 AA; 14007 MW; A7E709727BF91F46 CRC64;
MAGCSRCGDC LSACPEGIIV QGDGGFPTLN FSHGECTFCG ACADACSEPL FLPREQTPWQ
LVARIGEGCL AFGQVFCQAC QDSCEPRAIR FSPAPRGIPV PILTTADCTG CGACVSACPV
QAIRVTDSED ASHEA
//