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Protein

NAD(P)H-hydrate epimerase

Gene

Apoa1bp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.UniRule annotation1 Publication

Catalytic activityi

(6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.
(6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate.

Cofactori

K+Note: Binds 1 potassium ion per subunit.

Kineticsi

  1. KM=1.6 µM for (R)-NADHX1 Publication
  2. KM=0.33 µM for (R)-NADPHX1 Publication
  1. Vmax=0.26 µmol/min/mg enzyme toward (R)-NADHX1 Publication
  2. Vmax=1.2 µmol/min/mg enzyme toward (R)-NADPHX1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141PotassiumUniRule annotation
Metal bindingi179 – 1791PotassiumUniRule annotation
Binding sitei212 – 2121NAD(P)HXUniRule annotation
Metal bindingi215 – 2151PotassiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • protein homotetramerization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-binding, NAD, NADP, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDAi5.1.99.6. 3474.
ReactomeiR-MMU-197264. Nicotinamide salvaging.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)H-hydrate epimeraseUniRule annotation (EC:5.1.99.6)
Alternative name(s):
Apolipoprotein A-I-binding proteinUniRule annotation
Short name:
AI-BPUniRule annotation
NAD(P)HX epimeraseUniRule annotation
Gene namesi
Name:Apoa1bp
Synonyms:Aibp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2180167. Apoa1bp.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: MGI
  • cilium Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • extracellular region Source: MGI
  • extracellular space Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionUniRule annotationAdd
BLAST
Chaini54 – 282229NAD(P)H-hydrate epimerasePRO_0000292423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Phosphoserine; by PKACombined sources1 Publication
Modified residuei138 – 1381N6-succinyllysineCombined sources

Post-translational modificationi

Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation.UniRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K4Z3.
MaxQBiQ8K4Z3.
PaxDbiQ8K4Z3.
PRIDEiQ8K4Z3.
TopDownProteomicsiQ8K4Z3.

2D gel databases

REPRODUCTION-2DPAGEQ8K4Z3.

PTM databases

iPTMnetiQ8K4Z3.
PhosphoSiteiQ8K4Z3.
SwissPalmiQ8K4Z3.

Expressioni

Tissue specificityi

Detected in testis and sperm (at protein level). Expressed at high levels in heart, liver, kidney, and testis.1 Publication

Gene expression databases

BgeeiQ8K4Z3.
CleanExiMM_APOA1BP.
GenevisibleiQ8K4Z3. MM.

Interactioni

Subunit structurei

Interacts with APOA1 and APOA2 (By similarity). Homodimer.By similarity1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

DIPiDIP-59952N.
IntActiQ8K4Z3. 3 interactions.
MINTiMINT-1869651.
STRINGi10090.ENSMUSP00000029708.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 6712Combined sources
Turni68 – 703Combined sources
Helixi74 – 9219Combined sources
Helixi95 – 973Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi104 – 1096Combined sources
Helixi113 – 12715Combined sources
Beta strandi131 – 1355Combined sources
Helixi143 – 15412Combined sources
Beta strandi159 – 1624Combined sources
Helixi167 – 1737Combined sources
Beta strandi175 – 1817Combined sources
Helixi194 – 2029Combined sources
Beta strandi208 – 2136Combined sources
Turni219 – 2213Combined sources
Beta strandi230 – 2378Combined sources
Helixi240 – 2445Combined sources
Beta strandi247 – 2537Combined sources
Helixi259 – 2646Combined sources
Beta strandi277 – 2804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DG2X-ray2.45A/B/C/D/E/F25-282[»]
2O8NX-ray2.00A25-282[»]
3RNOX-ray2.50A25-282[»]
3RO7X-ray2.50A25-282[»]
3ROEX-ray2.11A/B/C/D/E/F25-282[»]
3ROGX-ray2.05A25-282[»]
3ROXX-ray2.40A25-282[»]
3ROZX-ray2.80A25-282[»]
ProteinModelPortaliQ8K4Z3.
SMRiQ8K4Z3. Positions 50-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8K4Z3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 269211YjeF N-terminalUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 1175NAD(P)HXUniRule annotation
Regioni183 – 1897NAD(P)HXUniRule annotation

Sequence similaritiesi

Belongs to the NnrE/AIBP family.UniRule annotation
Contains 1 YjeF N-terminal domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2585. Eukaryota.
COG0062. LUCA.
GeneTreeiENSGT00390000007227.
HOGENOMiHOG000174236.
HOVERGENiHBG058276.
InParanoidiQ8K4Z3.
KOiK17759.
OMAiHLGMFGY.
OrthoDBiEOG71K63V.
PhylomeDBiQ8K4Z3.
TreeFamiTF300197.

Family and domain databases

Gene3Di3.40.50.10260. 1 hit.
HAMAPiMF_01966. NADHX_epimerase.
InterProiIPR004443. YjeF_N_dom.
IPR032976. YJEFN_prot_eukaryotes.
[Graphical view]
PANTHERiPTHR13232. PTHR13232. 1 hit.
PfamiPF03853. YjeF_N. 1 hit.
[Graphical view]
SUPFAMiSSF64153. SSF64153. 1 hit.
TIGRFAMsiTIGR00197. yjeF_nterm. 1 hit.
PROSITEiPS51385. YJEF_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K4Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLRTLLGL GLLVAGSRLP RVISQQSVCR ARPIWWGTQR RGSETMAGAA
60 70 80 90 100
VKYLSQEEAQ AVDQELFNEY QFSVDQLMEL AGLSCATAIA KAYPPTSMSK
110 120 130 140 150
SPPTVLVICG PGNNGGDGLV CARHLKLFGY QPTIYYPKRP NKPLFTGLVT
160 170 180 190 200
QCQKMDIPFL GEMPPEPMMV DELYELVVDA IFGFSFKGDV REPFHSILSV
210 220 230 240 250
LSGLTVPIAS IDIPSGWDVE KGNPSGIQPD LLISLTAPKK SATHFTGRYH
260 270 280
YLGGRFVPPA LEKKYQLNLP SYPDTECVYR LQ
Length:282
Mass (Da):30,973
Last modified:October 1, 2002 - v1
Checksum:iDFD95155755D8D96
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ344092 mRNA. Translation: CAC86966.1.
AY566271 mRNA. Translation: AAT70236.1.
AK159846 mRNA. Translation: BAE35424.1.
BC058362 mRNA. Translation: AAH58362.1.
CCDSiCCDS17464.1.
RefSeqiNP_659146.1. NM_144897.3.
UniGeneiMm.205996.

Genome annotation databases

EnsembliENSMUST00000029708; ENSMUSP00000029708; ENSMUSG00000028070.
GeneIDi246703.
KEGGimmu:246703.
UCSCiuc008ptu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ344092 mRNA. Translation: CAC86966.1.
AY566271 mRNA. Translation: AAT70236.1.
AK159846 mRNA. Translation: BAE35424.1.
BC058362 mRNA. Translation: AAH58362.1.
CCDSiCCDS17464.1.
RefSeqiNP_659146.1. NM_144897.3.
UniGeneiMm.205996.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DG2X-ray2.45A/B/C/D/E/F25-282[»]
2O8NX-ray2.00A25-282[»]
3RNOX-ray2.50A25-282[»]
3RO7X-ray2.50A25-282[»]
3ROEX-ray2.11A/B/C/D/E/F25-282[»]
3ROGX-ray2.05A25-282[»]
3ROXX-ray2.40A25-282[»]
3ROZX-ray2.80A25-282[»]
ProteinModelPortaliQ8K4Z3.
SMRiQ8K4Z3. Positions 50-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59952N.
IntActiQ8K4Z3. 3 interactions.
MINTiMINT-1869651.
STRINGi10090.ENSMUSP00000029708.

PTM databases

iPTMnetiQ8K4Z3.
PhosphoSiteiQ8K4Z3.
SwissPalmiQ8K4Z3.

2D gel databases

REPRODUCTION-2DPAGEQ8K4Z3.

Proteomic databases

EPDiQ8K4Z3.
MaxQBiQ8K4Z3.
PaxDbiQ8K4Z3.
PRIDEiQ8K4Z3.
TopDownProteomicsiQ8K4Z3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029708; ENSMUSP00000029708; ENSMUSG00000028070.
GeneIDi246703.
KEGGimmu:246703.
UCSCiuc008ptu.1. mouse.

Organism-specific databases

CTDi246703.
MGIiMGI:2180167. Apoa1bp.

Phylogenomic databases

eggNOGiKOG2585. Eukaryota.
COG0062. LUCA.
GeneTreeiENSGT00390000007227.
HOGENOMiHOG000174236.
HOVERGENiHBG058276.
InParanoidiQ8K4Z3.
KOiK17759.
OMAiHLGMFGY.
OrthoDBiEOG71K63V.
PhylomeDBiQ8K4Z3.
TreeFamiTF300197.

Enzyme and pathway databases

BRENDAi5.1.99.6. 3474.
ReactomeiR-MMU-197264. Nicotinamide salvaging.

Miscellaneous databases

ChiTaRSiApoa1bp. mouse.
EvolutionaryTraceiQ8K4Z3.
PROiQ8K4Z3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K4Z3.
CleanExiMM_APOA1BP.
GenevisibleiQ8K4Z3. MM.

Family and domain databases

Gene3Di3.40.50.10260. 1 hit.
HAMAPiMF_01966. NADHX_epimerase.
InterProiIPR004443. YjeF_N_dom.
IPR032976. YJEFN_prot_eukaryotes.
[Graphical view]
PANTHERiPTHR13232. PTHR13232. 1 hit.
PfamiPF03853. YjeF_N. 1 hit.
[Graphical view]
SUPFAMiSSF64153. SSF64153. 1 hit.
TIGRFAMsiTIGR00197. yjeF_nterm. 1 hit.
PROSITEiPS51385. YJEF_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel apolipoprotein A-I-binding protein, AI-BP, secreted by cells of the kidney proximal tubules in response to HDL or ApoA-I."
    Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A., Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.
    Genomics 79:693-702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster.
  2. "Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation."
    Jha K.N., Shumilin I.A., Digilio L.C., Chertihin O., Zheng H., Schmitz G., Visconti P.E., Flickinger C.J., Minor W., Herr J.C.
    Endocrinology 149:2108-2120(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-282, SUBUNIT, PHOSPHORYLATION AT SER-43, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Testis.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair."
    Marbaix A.Y., Noel G., Detroux A.M., Vertommen D., Van Schaftingen E., Linster C.L.
    J. Biol. Chem. 286:41246-41252(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNNRE_MOUSE
AccessioniPrimary (citable) accession number: Q8K4Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.