ID A0A372JTS9_9ACTN Unreviewed; 413 AA.
AC A0A372JTS9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DZF91_02555 {ECO:0000313|EMBL:RFU43164.1};
OS Actinomadura logoneensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2293572 {ECO:0000313|EMBL:RFU43164.1, ECO:0000313|Proteomes:UP000261811};
RN [1] {ECO:0000313|EMBL:RFU43164.1, ECO:0000313|Proteomes:UP000261811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-G17 {ECO:0000313|EMBL:RFU43164.1,
RC ECO:0000313|Proteomes:UP000261811};
RA Shi L.;
RT "Actinomadura jelena sp. nov., a novel Actinomycete isolated from soil in
RT Chad.";
RL Submitted (AUG-2018) 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:RFU43164.1}.
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DR EMBL; QURH01000046; RFU43164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372JTS9; -.
DR OrthoDB; 9806925at2; -.
DR Proteomes; UP000261811; 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: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:0008152; P:metabolic process; 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 HAMAP; MF_01965; NADHX_dehydratase; 1.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR NCBIfam; TIGR00196; yjeF_cterm; 1.
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; 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 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:UP000261811}.
FT DOMAIN 1..132
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT DOMAIN 137..412
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU43164.1"
SQ SEQUENCE 413 AA; 41255 MW; 458165298B1F2B97 CRC64;
RAVAAGSRLH EGGLAELRAA GGRLVAIEDA RAAVAAADLV IDGLTGIGGT GALREPHASL
ARAASEAAGT VVACDVPSGV DASSGRVEGA AVRADVTVAF GTLKPGLLVD PGASYCGVVE
LVDIGLGPYL GDPDVVASTA EDVRPPLPGP ESDKYRRGVV GVLAGSTEFT GAAVLAVGGA
VHGGAGMVRF ASVPHAVELV RQRWPEAVTT VVEPGGKALE KIGRVQAWVV GPGLGTGQDA
EDLLGAVLST ELPVLVDADG LTVLARRRDL LARDAPTLLT PHAGELARLL GGDRAEIEAR
RLEWVRRAAA ELGATVLLKG STTVIAEPDR PVRVNPTGTP WLATAGTGDV LSGLTGALLA
GGMSALDAAA AGAYLHGLAA RLAAGGPFPD AGEAPVGAFD VITALPAAFR TLP
//
