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
//