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Database: UniProt
Entry: A0A2S6NKJ5_RHOGL
LinkDB: A0A2S6NKJ5_RHOGL
Original site: A0A2S6NKJ5_RHOGL 
ID   A0A2S6NKJ5_RHOGL        Unreviewed;        96 AA.
AC   A0A2S6NKJ5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Ferredoxin III {ECO:0000256|ARBA:ARBA00030616};
GN   ORFNames=CCS01_07360 {ECO:0000313|EMBL:PPQ35491.1};
OS   Rhodopila globiformis (Rhodopseudomonas globiformis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Rhodopila.
OX   NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ35491.1, ECO:0000313|Proteomes:UP000239724};
RN   [1] {ECO:0000313|EMBL:PPQ35491.1, ECO:0000313|Proteomes:UP000239724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ35491.1,
RC   ECO:0000313|Proteomes:UP000239724};
RX   PubMed=29423563;
RA   Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT   "New insights into the metabolic potential of the phototrophic purple
RT   bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT   and evidence for a vanadium-dependent nitrogenase.";
RL   Arch. Microbiol. 0:0-0(2018).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000256|ARBA:ARBA00003532}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:PPQ35491.1}.
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DR   EMBL; NHRY01000072; PPQ35491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6NKJ5; -.
DR   OrthoDB; 9810688at2; -.
DR   Proteomes; UP000239724; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014283; FdIII_4_nif.
DR   NCBIfam; TIGR02936; fdxN_nitrog; 1.
DR   PANTHER; PTHR43687:SF5; 4FE-4S FERREDOXIN-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          15..44
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          67..96
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   96 AA;  10298 MW;  7BFF094FD6FE2870 CRC64;
     MTQLTRDGRP WEPQYLLGID AKVCIGCGRC YKVCSRNVMT LAGIDEDGEF VDIGADDDDA
     DEIERKVMIM RDAGGCIGCG ACARVCPTNA QSHGPA
//
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