ID A0A2K6SHT7_SAIBB Unreviewed; 288 AA.
AC A0A2K6SHT7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_03159};
DE AltName: Full=Apolipoprotein A-I-binding protein {ECO:0000256|HAMAP-Rule:MF_03159};
DE Short=AI-BP {ECO:0000256|HAMAP-Rule:MF_03159};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
GN Name=NAXE {ECO:0000313|Ensembl:ENSSBOP00000006957.1};
GN Synonyms=AIBP {ECO:0000256|HAMAP-Rule:MF_03159}, APOA1BP
GN {ECO:0000256|HAMAP-Rule:MF_03159};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000006957.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000006957.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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.
CC {ECO:0000256|HAMAP-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 Evidence={ECO:0000256|HAMAP-Rule:MF_03159};
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|HAMAP-Rule:MF_03159};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03159};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03159};
CC -!- SUBUNIT: Homodimer. Interacts with APOA1 and APOA2. {ECO:0000256|HAMAP-
CC Rule:MF_03159}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159}.
CC Secreted {ECO:0000256|HAMAP-Rule:MF_03159}. Note=In sperm, secretion
CC gradually increases during capacitation. {ECO:0000256|HAMAP-
CC Rule:MF_03159}.
CC -!- PTM: Undergoes physiological phosphorylation during sperm capacitation,
CC downstream to PKA activation. {ECO:0000256|HAMAP-Rule:MF_03159}.
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC Rule:MF_03159}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03159}.
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DR RefSeq; XP_003937893.1; XM_003937844.2.
DR AlphaFoldDB; A0A2K6SHT7; -.
DR STRING; 39432.ENSSBOP00000006957; -.
DR Ensembl; ENSSBOT00000023709.1; ENSSBOP00000006957.1; ENSSBOG00000020449.1.
DR GeneID; 101032133; -.
DR KEGG; sbq:101032133; -.
DR CTD; 128240; -.
DR GeneTree; ENSGT00390000007227; -.
DR OMA; RHLFHYG; -.
DR OrthoDB; 1493at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031580; P:membrane raft distribution; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:Ensembl.
DR GO; GO:0010874; P:regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 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 NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1.
DR PANTHER; PTHR13232:SF11; NAD(P)H-HYDRATE EPIMERASE; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03159};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03159};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03159}; NAD {ECO:0000256|HAMAP-Rule:MF_03159};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03159};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_03159};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_03159};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..288
FT /note="NAD(P)H-hydrate epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014422309"
FT DOMAIN 65..275
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT BINDING 119..123
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 120
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 189..195
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 218
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
SQ SEQUENCE 288 AA; 31645 MW; 103D3A5D30B34911 CRC64;
MSGLRALLGL GLLVAGSRLQ RITTQTSACR SGPTWWGPQR LNSGVRWNSE VMASTAVKYL
SQEEAQAVDQ ELFNEYQFSV DQLMELAGLS CATAIAKAYP PTSMSRSPPT VLVICGPGNN
GGDGLVCARH LKLFGYQPTI YYPKRPNKPL FTALVTQCQK MDIPFLGEMP SEPTVIDELY
ELVVDAIFGF SFKGDVREPF HSILSVLKGL TVPIASIDIP SGWDVEKGNP AGIQPDLLIS
LTAPKKSATQ FTGRYHYLGG RFVPPALEKK YQLNLPPYPD TECVYRLR
//
