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).
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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
//