NNRE_BOVIN
ID NNRE_BOVIN Reviewed; 288 AA.
AC Q6QRN6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blastocyst;
RX PubMed=15278903; DOI=10.1002/mrd.20156;
RA Hwang K.-C., Cui X.-S., Park S.-P., Shin M.-R., Park S.-Y., Kim E.-Y.,
RA Kim N.-H.;
RT "Identification of differentially regulated genes in bovine blastocysts
RT using an annealing control primer system.";
RL Mol. Reprod. Dev. 69:43-51(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-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; AY528250; AAS20598.1; -; mRNA.
DR EMBL; BC114830; AAI14831.1; -; mRNA.
DR RefSeq; NP_991365.1; NM_205796.3.
DR RefSeq; XP_005203675.1; XM_005203618.3.
DR AlphaFoldDB; Q6QRN6; -.
DR SMR; Q6QRN6; -.
DR STRING; 9913.ENSBTAP00000000518; -.
DR PaxDb; Q6QRN6; -.
DR PeptideAtlas; Q6QRN6; -.
DR PRIDE; Q6QRN6; -.
DR GeneID; 404132; -.
DR KEGG; bta:404132; -.
DR CTD; 128240; -.
DR eggNOG; KOG2585; Eukaryota.
DR HOGENOM; CLU_024853_3_0_1; -.
DR InParanoid; Q6QRN6; -.
DR OrthoDB; 1030667at2759; -.
DR TreeFam; TF300197; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Phosphoprotein; Potassium; Reference proteome;
KW Secreted; Transit peptide; Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT CHAIN 33..288
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000292422"
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 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4Z3"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4Z3"
SQ SEQUENCE 288 AA; 31363 MW; DEA84926DB23D8CE CRC64;
MSGLRALLGL GLLVAGSRLS RVRVQAGSCR AGATWWVPQR LISGGRGDSE VMASSAVKYL
SQEEAQAVDQ ELFNEYQFSV DQLMELAGLS CATAIAKAYP PTSLSRSPPT VLVICGPGNN
GGDGLVCARH LKLFGYQPTI YYPKRPNKPL FTALVTQCQK MDIPFLGEMP PEPMLIDELY
ELVVDAIFGF SFTGEVREPF RSILSVLNGL TVPIASIDIP SGWDVEKGSS GGIQPDLLIS
LTAPKKSATQ FTGRYHYLGG RFVPPALEKK YQLNLPPYPD TECVYRLQ
