ID W8TEI7_PEPAC Unreviewed; 508 AA.
AC W8TEI7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme {ECO:0000256|PIRNR:PIRNR017184};
DE AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|PIRNR:PIRNR017184};
DE Includes:
DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|PIRNR:PIRNR017184};
DE EC=4.2.1.136 {ECO:0000256|PIRNR:PIRNR017184};
DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|PIRNR:PIRNR017184};
DE Includes:
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|PIRNR:PIRNR017184};
DE EC=5.1.99.6 {ECO:0000256|PIRNR:PIRNR017184};
GN Name=yjeF {ECO:0000313|EMBL:AHM56223.1};
GN Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}, nnrE
GN {ECO:0000256|HAMAP-Rule:MF_01966};
GN ORFNames=EAL2_c09240 {ECO:0000313|EMBL:AHM56223.1};
OS Peptoclostridium acidaminophilum DSM 3953.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM56223.1, ECO:0000313|Proteomes:UP000019591};
RN [1] {ECO:0000313|EMBL:AHM56223.1, ECO:0000313|Proteomes:UP000019591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM56223.1,
RC ECO:0000313|Proteomes:UP000019591};
RX PubMed=24926057;
RA Poehlein A., Andreesen J.R., Daniel R.;
RT "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT acidaminophilum al-2 (DSM 3953).";
RL Genome Announc. 2:e00573-14(2014).
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, ECO:0000256|PIRNR:PIRNR017184}.
CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC expense of ADP, which is converted to AMP. Together with NAD(P)HX
CC epimerase, which catalyzes the epimerization of the S- and R-forms, the
CC enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of
CC NAD(P)H that is a result of enzymatic or heat-dependent hydration.
CC {ECO:0000256|HAMAP-Rule:MF_01965}.
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|ARBA:ARBA00000013, ECO:0000256|HAMAP-
CC Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
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|ARBA:ARBA00000909, ECO:0000256|HAMAP-
CC Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
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, ECO:0000256|HAMAP-
CC Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
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, ECO:0000256|HAMAP-
CC Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
CC ECO:0000256|PIRNR:PIRNR017184};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01965};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC Rule:MF_01965}.
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC Rule:MF_01966}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
CC family. {ECO:0000256|ARBA:ARBA00009524, ECO:0000256|PIRNR:PIRNR017184}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC {ECO:0000256|ARBA:ARBA00006001, ECO:0000256|PIRNR:PIRNR017184}.
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; CP007452; AHM56223.1; -; Genomic_DNA.
DR AlphaFoldDB; W8TEI7; -.
DR STRING; 1286171.EAL2_c09240; -.
DR KEGG; eac:EAL2_c09240; -.
DR PATRIC; fig|1286171.3.peg.874; -.
DR eggNOG; COG0062; Bacteria.
DR eggNOG; COG0063; Bacteria.
DR HOGENOM; CLU_024853_4_1_9; -.
DR OrthoDB; 9806925at2; -.
DR Proteomes; UP000019591; Chromosome.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR017953; Carbohydrate_kinase_pred_CS.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR030677; Nnr.
DR InterPro; IPR001763; Rhodanese-like_dom.
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 NCBIfam; TIGR00197; yjeF_nterm; 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 PIRSF; PIRSF017184; Nnr; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 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, ECO:0000256|HAMAP-
KW Rule:MF_01965};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01966}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01965};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
KW Reference proteome {ECO:0000313|Proteomes:UP000019591};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 10..220
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT DOMAIN 23..97
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 227..501
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT BINDING 58..62
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 59
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 128
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 132..138
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 163
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 166
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 263
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 326
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 375
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 412..416
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 441
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 442
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ SEQUENCE 508 AA; 53731 MW; 7EEE748FF75FAB5F CRC64;
MKKIAYSFEM RNLDKTTIEA YGIPGAVLME NAGRKTYEQI EELAGNEKKI LVVCGRGNNG
GDGYVIARHL HNNGYTVSVS LIGGRDGIKG DALLNLEIIE RMGIQIDYIA NAEDFAAVLK
RGYDIIVDAI FGIGIDRKVA QPFAEIIELI NSYEKKELVV AVDLPSGLNT DTGEIMGSAV
QSDITVTFGA LKPANIFNEG INLCGKTVVA DISIPRELLE AERKSLLESG FCAGIIRRRK
CSSHKGTYGK VGIVGGSLNM PGAAILSSRA AMRMGSGIVN VFADCEAFSA LSGKTPEVIV
VKSDYSRPKD VTEELAGLDA VLVGPGLSKA AGRRELLLEV LSAYEGPLAI DADGLNLLQG
ELGTLRGKNA IITPHIGEMA RLAGKESSFV SHNAMEVARE FAAEYGCVVV LKSASTVIAL
PEGEIFVCSS PNPGMATAGS GDVLSGAIVS LLGQGYEPRE AALLGVHIHS LAGRLALYKK
GEYGLLAGDI VEEMPEAVKG LLEIKDGF
//
