ID A0A151NY56_ALLMI Unreviewed; 866 AA.
AC A0A151NY56;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=APOA1BP {ECO:0000256|HAMAP-Rule:MF_03159};
GN Synonyms=AIBP {ECO:0000256|HAMAP-Rule:MF_03159};
GN ORFNames=Y1Q_0004501 {ECO:0000313|EMBL:KYO41806.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO41806.1};
RN [1] {ECO:0000313|EMBL:KYO41806.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO41806.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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_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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159}.
CC Secreted {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO41806.1}.
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DR EMBL; AKHW03001603; KYO41806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NY56; -.
DR eggNOG; KOG2585; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR024812; TPR_24.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR47050; TETRATRICOPEPTIDE REPEAT PROTEIN 24; 1.
DR PANTHER; PTHR47050:SF2; TETRATRICOPEPTIDE REPEAT PROTEIN 24; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; TPR-like; 2.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS50005; TPR; 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|HAMAP-Rule:MF_03159};
KW 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:UP000050525};
KW Secreted {ECO:0000256|HAMAP-Rule:MF_03159};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 227..260
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 643..853
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 697..701
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 698
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 763
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 767..773
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 796
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 799
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
SQ SEQUENCE 866 AA; 93948 MW; 6A78997186A36542 CRC64;
MKKKEEKAKA LGEAEKEEDR SLRSRAEIES LTKAGHQALL VGDAQEALAC FKKAFLLSLD
APNPQVQKAC AFNVGAAYVE SGKPEKGLEF LLKSRPTEGE AVEHLGDLYF NLGAAHEGLQ
DFPKALEYFR KASGHYCSTQ AGNQAGACMK MGYCYLGMQD STRAAQCFQQ AGLAYAEAQS
LEAAALALNE ASNCMLQSQQ YGAGEIVEVL NKCRLLCEDI GGKALLERLY NDMGLSYSQL
KIFSLAAESF ERALLLCQTD PGDRRKEAVV LQNLGAAHNT LGNFHLALEL HQRAASLHSV
LGNRKAQGQC FSNLAYAFSQ LDDHEAAGEN YLHALQAFKD VDDLLGQWQA CEGLGASCFH
LRDPEKAVMH YKEALMLLSK CQDASETAQE RIVNKLADAV QYKLSLDSRA CHRGSLAPAA
PLKHFPGKLQ TSSQVRFSAA LHHEKGREPQ TPRQGNHLLP PAQPQEELSS SLLAALVPQR
PSPPRGAAGV PWQAGRQPLQ RPSLRASDAG LAAQTAGLAE GCQLEPRDPS CHVALGSSHM
QEVDASSRAP MYYNQPQANS NLNNTYLHPD PYYHNCLQNG RLQPSLKSLL PTPLATSPVK
GRSPGGGRRG AGSSPSYAHS CEAAPIVGTS QRLKGWHIRQ QEAQAIDQEL FTEYKFSVDQ
LMELAGLSCA TAIAKAYPPG SFTKPQPTVL VVCGPGNNGG DGLVCARHLK LFGYEPTVYY
PKRPSKALFE DLTTQCQKMD IPFLPEFPAE AMLIDELYGL VVDAIFGFSF QGAVREPFGS
ILKTLAQVTV PIASIDIPSG WDVEKGNPDG LQPDMLISLT APKAAARHFT GRYHFLGGRF
VPAALERKYG LNLPAYPGTD CTLQLM
//
