NNRE_PIG
ID NNRE_PIG Reviewed; 288 AA.
AC Q0PIT9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6;
DE AltName: Full=Apolipoprotein A-I-binding protein {ECO:0000255|HAMAP-Rule:MF_03159};
DE Short=AI-BP {ECO:0000255|HAMAP-Rule:MF_03159};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000250|UniProtKB:Q8NCW5};
DE Flags: Precursor;
GN Name=NAXE {ECO:0000250|UniProtKB:Q8NCW5};
GN Synonyms=AIBP {ECO:0000255|HAMAP-Rule:MF_03159},
GN APOA1BP {ECO:0000255|HAMAP-Rule:MF_03159};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang T., Xiong Y.-Z., Huang J.-S., Xu D.-Q.;
RT "Cloning and sequence analysis of pig AIBP gene.";
RL Submitted (JUN-2006) 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. Accelerates cholesterol efflux from endothelial cells to
CC high-density lipoprotein (HDL) and thereby regulates angiogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q8NCW5, ECO:0000255|HAMAP-
CC Rule:MF_03159}.
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 -!- 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03159};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03159};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with APOA1 and APOA2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4Z3,
CC ECO:0000250|UniProtKB:Q8NCW5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}.
CC Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion
CC gradually increases during capacitation. {ECO:0000255|HAMAP-
CC Rule:MF_03159}.
CC -!- PTM: Undergoes physiological phosphorylation during sperm capacitation,
CC downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159}.
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC Rule:MF_03159}.
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DR EMBL; DQ826508; ABH01264.1; -; mRNA.
DR RefSeq; NP_001072132.1; NM_001078664.1.
DR AlphaFoldDB; Q0PIT9; -.
DR SMR; Q0PIT9; -.
DR STRING; 9823.ENSSSCP00000006906; -.
DR PaxDb; Q0PIT9; -.
DR PeptideAtlas; Q0PIT9; -.
DR PRIDE; Q0PIT9; -.
DR GeneID; 780405; -.
DR KEGG; ssc:780405; -.
DR CTD; 128240; -.
DR eggNOG; KOG2585; Eukaryota.
DR InParanoid; Q0PIT9; -.
DR OrthoDB; 1030667at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0031580; P:membrane raft distribution; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; ISS:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.10260; -; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR PANTHER; PTHR13232; PTHR13232; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Lipid transport; Metal-binding; Mitochondrion; NAD; NADP;
KW Nucleotide-binding; Potassium; Reference proteome; Secreted;
KW Transit peptide; Transport.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT CHAIN 60..288
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000292424"
FT DOMAIN 65..275
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 119..123
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 120
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 189..195
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 218
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4Z3"
SQ SEQUENCE 288 AA; 31501 MW; C0E945E3EDF22385 CRC64;
MSGLRALLGL GLPVAGSRLP RVRVQAGACR ARPTWWGPQR LISGGRGDVE GMASSAVKYL
SQEEAQAVDQ ELFNEYQFSV DQLMELAGLS CATAIAKVYP PTSLSRSPPT VLVICGPGNN
GGDGLVCARH LKLFGYHPTI YYPKRPNKPL FTALVTQCQK MDIPFLDEMP SEPTLIDELY
ELVVDAIFGF SFKGEVREPF RSILSVLNGL TVPIASIDIP SGWDVERGNS GGIQPDLLIS
LTAPKKSAAQ FTGRYHYLGG RFVPPALEKK YQLNLPPYPD TECVYRLQ
