GenomeNet

Database: UniProt
Entry: D2TS77_CITRI
LinkDB: D2TS77_CITRI
Original site: D2TS77_CITRI 
ID   D2TS77_CITRI            Unreviewed;       369 AA.
AC   D2TS77;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=2Fe-2S iron-sulfur cluster binding protein {ECO:0000313|EMBL:CBG87788.1};
GN   OrderedLocusNames=ROD_10091 {ECO:0000313|EMBL:CBG87788.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG87788.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG87788.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG87788.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG87788.1; -; Genomic_DNA.
DR   RefSeq; WP_012905332.1; NC_013716.1.
DR   AlphaFoldDB; D2TS77; -.
DR   STRING; 637910.ROD_10091; -.
DR   KEGG; cro:ROD_10091; -.
DR   eggNOG; COG0633; Bacteria.
DR   eggNOG; COG3217; Bacteria.
DR   HOGENOM; CLU_028286_0_2_6; -.
DR   OrthoDB; 581532at2; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR005303; MOCOS_middle.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   PANTHER; PTHR36930; METAL-SULFUR CLUSTER BIOSYNTHESIS PROTEINS YUAD-RELATED; 1.
DR   PANTHER; PTHR36930:SF1; MOSC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   4: Predicted;
FT   DOMAIN          115..264
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
FT   DOMAIN          289..369
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   369 AA;  40260 MW;  784FE66E20C46FE9 CRC64;
     MLTLTRLFIH PVKSMRGIGL THALADVSGL AFDRIFMITE TDGTFITARQ YPQMVRFTPS
     PLHDGLHLTA PDGSSAVARF SDFAAQDAPT EVWGNHFTAR IAPDAINQWL SGFFSRDVQL
     RWVGPQLTRR VKRHAGVPLS FADGYPYLLV NDASLRDLQR RCPAGVQVEQ FRPNIVVSGA
     SAWEEDTWKA IRIGEVVFDV VKPCSRCIFT TVSPEKGLKH PSGEPLATLQ CFRTAPDNGD
     VDFGQNLIAR NSGVIRVGDE VEILSTGPAR VYGAARQDDT VAVAPQADAA VDIDWQGQAF
     RGNNQQVLLE QLESQGIRIP YSCRTGICGS CRIKLLEGEV SPLKKSALGA DGTILSCSCV
     PKTALKLAR
//
DBGET integrated database retrieval system