YDEP_ECOL6
ID YDEP_ECOL6 Reviewed; 759 AA.
AC Q8FHF8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein YdeP;
GN Name=ydeP; OrderedLocusNames=c1930;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Probably involved in acid resistance. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- INDUCTION: By EvgA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE014075; AAN80388.1; -; Genomic_DNA.
DR RefSeq; WP_000726730.1; NC_004431.1.
DR AlphaFoldDB; Q8FHF8; -.
DR SMR; Q8FHF8; -.
DR STRING; 199310.c1930; -.
DR EnsemblBacteria; AAN80388; AAN80388; c1930.
DR KEGG; ecc:c1930; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_16_1_6; -.
DR OMA; PRSLKCH; -.
DR BioCyc; ECOL199310:C1930-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR PANTHER; PTHR43105:SF4; PTHR43105:SF4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01701; Fdhalpha-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase.
FT CHAIN 1..759
FT /note="Protein YdeP"
FT /id="PRO_0000063228"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 759 AA; 83691 MW; 2EEB319EDE20DE34 CRC64;
MKKKIESYQG AAGGWGAVKS VANAVRKQMD IRQDVIAMFD MNKPEGFDCP GCAWPDPKHS
ASFDICENGA KAIAWEVTDK QVNASFFAEN TVQSLLTWGD HELEAAGRLT QPLKYDDVSD
CYKPLSWQQA FDEIGARLQS YSDPNQVEFY TSGRTSNEAA FLYQLFAREY RSNNFPDCSN
MCHEPTSVGL AASIGVGKGT VLLEDFEKCD LVICIGHNPG TNHPRMLTSL RALVKRGAKM
IAINPLQERG LERFTAPQNP FEMLTNSETQ LASAYYNVRI GGDMALLKGM MRLLIERDDA
ASAAGRPSLL DDEFIQTHTV GFDELRRDVL NSEWKDIERI SGLSQTQIAE LADAYAAAER
TIICYGMGIT QHEHGTQNVQ QLVNLLLMKG NIGKPGAGIC PLRGHSNVQG DRTVGITEKP
SAEFLDRLCE RYGFTPPHAP GHAAIASMQA ICTGQARALI CMGGNFALAM PDREASAVPL
TQLDLAVHVA TKLNRSHLLT ARHSYILPVL GRSEIDMQKS GAQAVTVEDS MSMIHASRGV
LKPAGVMLKS ECAVVAGIAQ AALPQSVVAW EYLVEDYDRI RNDIEAVLPE FADYNQRIRH
PGGFHLINAA AERRWMTSSG KANFITSKGL LEDPSSAFNS KLVMATVRSH DQYNTTIYGM
DDRYRGVFGQ RDVVFMSAKQ AKICRVKNGE RVNLIALTPD GKRSSRRMDR LKVVIYPMAD
RSLVTYFPES NHMLTLDNHD PLSGIPGYKS IPVELEPSN