ID A0A021VRU1_9CELL Unreviewed; 376 AA.
AC A0A021VRU1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme Nnr {ECO:0000256|ARBA:ARBA00018591};
DE EC=4.2.1.136 {ECO:0000256|ARBA:ARBA00013129};
DE AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|ARBA:ARBA00032624};
DE Flags: Fragment;
GN ORFNames=N866_15835 {ECO:0000313|EMBL:EYR61817.1};
OS Actinotalea ferrariae CF5-4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Actinotalea.
OX NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR61817.1, ECO:0000313|Proteomes:UP000019753};
RN [1] {ECO:0000313|EMBL:EYR61817.1, ECO:0000313|Proteomes:UP000019753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-4 {ECO:0000313|EMBL:EYR61817.1,
RC ECO:0000313|Proteomes:UP000019753};
RA Chen F., Li Y., Wang G.;
RT "Actinotalea ferrariae CF5-4.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of the
CC S- and R-forms of NAD(P)HX and the dehydration of the S-form of
CC NAD(P)HX at the expense of ADP, which is converted to AMP. This allows
CC the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that
CC is a result of enzymatic or heat-dependent hydration.
CC {ECO:0000256|ARBA:ARBA00025153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
CC Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=4.2.1.136;
CC Evidence={ECO:0000256|ARBA:ARBA00001026};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
CC Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=4.2.1.136;
CC Evidence={ECO:0000256|ARBA:ARBA00001241};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
CC family. {ECO:0000256|ARBA:ARBA00009524}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC {ECO:0000256|ARBA:ARBA00006001}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYR61817.1}.
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DR EMBL; AXCW01000496; EYR61817.1; -; Genomic_DNA.
DR RefSeq; WP_034229822.1; NZ_AXCW01000496.1.
DR AlphaFoldDB; A0A021VRU1; -.
DR OrthoDB; 9806925at2; -.
DR Proteomes; UP000019753; Unassembled WGS sequence.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01171; YXKO-related; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR InterPro; IPR017953; Carbohydrate_kinase_pred_CS.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR PANTHER; PTHR12592:SF0; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE; 1.
DR PANTHER; PTHR12592; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER; 1.
DR Pfam; PF01256; Carb_kinase; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS01050; YJEF_C_2; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Kinase {ECO:0000313|EMBL:EYR61817.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019753};
KW Transferase {ECO:0000313|EMBL:EYR61817.1}.
FT DOMAIN 1..133
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT DOMAIN 144..376
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EYR61817.1"
FT NON_TER 376
FT /evidence="ECO:0000313|EMBL:EYR61817.1"
SQ SEQUENCE 376 AA; 37667 MW; 7E8FED195696F6F3 CRC64;
PAPASGASGV DWLGDALAEA AAADVVLDGL LGIGARGGLR GTAAEVVRLL AEVLGQLESV
GAGHVAALRP AVVAVDLPSG LAVDTGAVPG PVLPADLTVT FGVPKPGLLL PPAAHLVGRL
EVVDLGLRPV LAERSVAPAL VRLGAADLAG LWPVPGPGAH KYSRGVVGVV AGTATYPGAA
VLTVAGAQGA GCGMVRYVGP DRVREAVVAA HPEVVTGSDA QVRVQAWVLG PGLDPADEDQ
ADRARAALAG AVAEHLPVVV DAGALWLLPD RVPPRVVLTP HAGELARLLQ GRWVDVDRED
VEAEPLRWAR EAHDRTGATV LLKGAVSVVV GPHGAYAQAD APPWLATAGA GDVLAGILGA
LLAGRADLDA PDDPAR
//
