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Database: UniProt
Entry: M5BBE3_9MICO
LinkDB: M5BBE3_9MICO
Original site: M5BBE3_9MICO 
ID   M5BBE3_9MICO            Unreviewed;       230 AA.
AC   M5BBE3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
DE            EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_01966};
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
GN   Name=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN   ORFNames=CMN_01905 {ECO:0000313|EMBL:CCE75850.1};
OS   Clavibacter nebraskensis NCPPB 2581.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE75850.1, ECO:0000313|Proteomes:UP000012170};
RN   [1] {ECO:0000313|EMBL:CCE75850.1, ECO:0000313|Proteomes:UP000012170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA   Gartemann K.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCE75850.1, ECO:0000313|Proteomes:UP000012170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA   Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S.,
RA   Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A.,
RA   Eichenlaub R., Rueckert C.;
RT   "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp.
RT   nebraskensis.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
CC       NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or
CC       heat-dependent hydration. This is a prerequisite for the S-specific
CC       NAD(P)H-hydrate dehydratase to allow the repair of both epimers of
CC       NAD(P)HX. {ECO:0000256|HAMAP-Rule:MF_01966}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
CC         ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
CC         ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01966};
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01966}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
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DR   EMBL; HE614873; CCE75850.1; -; Genomic_DNA.
DR   RefSeq; WP_015490587.1; NC_020891.1.
DR   AlphaFoldDB; M5BBE3; -.
DR   KEGG; cmc:CMN_01905; -.
DR   PATRIC; fig|1097677.3.peg.1626; -.
DR   HOGENOM; CLU_024853_0_2_11; -.
DR   Proteomes; UP000012170; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR   HAMAP; MF_01966; NADHX_epimerase; 1.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   NCBIfam; TIGR00197; yjeF_nterm; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01966};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01966};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01966};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01966};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01966}.
FT   DOMAIN          11..223
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   BINDING         59..63
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         60
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         125
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         165
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         168
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   230 AA;  22569 MW;  B646C67BB10330D4 CRC64;
     MSDIASIADG YAAADIRAAE APLLAAGAQL MRVAAAGLAR VCRAEAPDGA VLVLVGAGNN
     GGDALLAAAE LARDGREVRV IRTASRIHEV GAARVAAAGV PITPSEELDD AGVAALGRAS
     ALVVDGILGI GTTASPALRG EARRVVAALL GIVRDAGGPV VVACDIPSGV GCDDGQVPDP
     TVLPADVTVT FGAGKPGLMR GPGRALAGRV ELVDVGLDLS GTMPRARAAP
//
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