NUD16_MOUSE
ID NUD16_MOUSE Reviewed; 195 AA.
AC Q6P3D0; Q9D716;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=U8 snoRNA-decapping enzyme;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q96DE0};
DE AltName: Full=IDP phosphatase {ECO:0000303|PubMed:20385596};
DE Short=IDPase;
DE EC=3.6.1.64 {ECO:0000269|PubMed:20385596};
DE AltName: Full=Inosine diphosphate phosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 16;
DE Short=Nudix motif 16;
DE AltName: Full=m7GpppN-mRNA hydrolase;
GN Name=Nudt16;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION IN MRNA DEGRADATION ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
RA Song M.G., Li Y., Kiledjian M.;
RT "Multiple mRNA decapping enzymes in mammalian cells.";
RL Mol. Cell 40:423-432(2010).
RN [5]
RP FUNCTION AS AN IDP PHOSPHATASE.
RX PubMed=20081199; DOI=10.1093/nar/gkp1250;
RA Abolhassani N., Iyama T., Tsuchimoto D., Sakumi K., Ohno M., Behmanesh M.,
RA Nakabeppu Y.;
RT "NUDT16 and ITPA play a dual protective role in maintaining chromosome
RT stability and cell growth by eliminating dIDP/IDP and dITP/ITP from
RT nucleotide pools in mammals.";
RL Nucleic Acids Res. 38:2891-2903(2010).
RN [6]
RP FUNCTION AS AN IDP PHOSPHATASE, AND CATALYTIC ACTIVITY.
RX PubMed=20385596; DOI=10.1093/nar/gkq249;
RA Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.;
RT "NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces
RT accumulation of single-strand breaks in nuclear DNA and growth arrest.";
RL Nucleic Acids Res. 38:4834-4843(2010).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32432673; DOI=10.1093/nar/gkaa402;
RA Sharma S., Grudzien-Nogalska E., Hamilton K., Jiao X., Yang J., Tong L.,
RA Kiledjian M.;
RT "Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs.";
RL Nucleic Acids Res. 48:6788-6798(2020).
CC -!- FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage
CC of the cap structure of snoRNAs and mRNAs in a metal-dependent manner.
CC Part of the U8 snoRNP complex that is required for the accumulation of
CC mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G
CC and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the
CC RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does
CC not hydrolyze cap analog structures like 7-methylguanosine nucleoside
CC triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs
CC but with less efficiencies. Has broad substrate specificity with
CC manganese or cobalt as cofactor and can act on various RNA species.
CC Binds to the U8 snoRNA; metal is not required for RNA-binding. May play
CC a role in the regulation of snoRNAs and mRNAs degradation (By
CC similarity). Acts also as a phosphatase; hydrolyzes the non-canonical
CC purine nucleotides inosine diphosphate (IDP) and deoxyinosine
CC diphosphate (dITP) as well as guanosine diphosphate (GDP),
CC deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine
CC triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their
CC respective monophosphate derivatives and does not distinguish between
CC the deoxy- and ribose forms. The order of activity with different
CC substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds
CC strongly to GTP, ITP and XTP. Participates in the hydrolysis of
CC dIDP/IDP and probably excludes non-canonical purines from RNA and DNA
CC precursor pools, thus preventing their incorporation into RNA and DNA
CC and avoiding chromosomal lesions. Exhibits decapping activity towards
CC NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping
CC activity towards dpCoA-capped RNAs in vitro (PubMed:32432673).
CC {ECO:0000250|UniProtKB:Q96DE0, ECO:0000269|PubMed:20081199,
CC ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968,
CC ECO:0000269|PubMed:32432673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.64;
CC Evidence={ECO:0000269|PubMed:20385596};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC Evidence={ECO:0000269|PubMed:20385596};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dIDP + H2O = dIMP + H(+) + phosphate; Xref=Rhea:RHEA:35211,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61194, ChEBI:CHEBI:62286; EC=3.6.1.64;
CC Evidence={ECO:0000269|PubMed:20385596};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35212;
CC Evidence={ECO:0000269|PubMed:20385596};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-ribonucleoside in mRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end
CC phospho-adenosine-phospho-ribonucleoside in mRNA + FMN + 2 H(+);
CC Xref=Rhea:RHEA:67588, Rhea:RHEA-COMP:15719, Rhea:RHEA-COMP:17275,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:144051, ChEBI:CHEBI:172372;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67589;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-
CC phosphopantetheine + a 5'-end phospho-adenosine-phospho-
CC ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-
CC COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000305|PubMed:32432673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593;
CC Evidence={ECO:0000305|PubMed:32432673};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96DE0};
CC Note=Binds 3 or 4 divalent metal cations. Acts specifically on U8
CC snoRNA with magnesium as cofactor. Has broad substrate specificity with
CC bound manganese or cobalt (in vitro). {ECO:0000250|UniProtKB:Q96DE0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96DE0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96DE0}. Note=Localized predominantly in the
CC cytoplasm. Localized in nucleolus, and in a minor proportion in
CC distinct foci in the nucleoplasm. {ECO:0000250|UniProtKB:Q6TEC1,
CC ECO:0000250|UniProtKB:Q96DE0}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, spleen, lung, heart,
CC liver, kidney and muscle (at protein level).
CC {ECO:0000269|PubMed:21070968}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NUDT16 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26469.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009737; BAB26469.1; ALT_FRAME; mRNA.
DR EMBL; BC064048; AAH64048.1; -; mRNA.
DR CCDS; CCDS40751.1; -.
DR RefSeq; NP_083661.2; NM_029385.2.
DR AlphaFoldDB; Q6P3D0; -.
DR SMR; Q6P3D0; -.
DR STRING; 10090.ENSMUSP00000035179; -.
DR iPTMnet; Q6P3D0; -.
DR PhosphoSitePlus; Q6P3D0; -.
DR EPD; Q6P3D0; -.
DR MaxQB; Q6P3D0; -.
DR PaxDb; Q6P3D0; -.
DR PeptideAtlas; Q6P3D0; -.
DR PRIDE; Q6P3D0; -.
DR ProteomicsDB; 295542; -.
DR DNASU; 75686; -.
DR Ensembl; ENSMUST00000035179; ENSMUSP00000035179; ENSMUSG00000032565.
DR GeneID; 75686; -.
DR KEGG; mmu:75686; -.
DR UCSC; uc009rhv.1; mouse.
DR CTD; 131870; -.
DR MGI; MGI:1922936; Nudt16.
DR VEuPathDB; HostDB:ENSMUSG00000032565; -.
DR eggNOG; ENOG502S20E; Eukaryota.
DR GeneTree; ENSGT00390000016224; -.
DR HOGENOM; CLU_110418_0_1_1; -.
DR InParanoid; Q6P3D0; -.
DR OMA; HVMLYCD; -.
DR OrthoDB; 1385294at2759; -.
DR PhylomeDB; Q6P3D0; -.
DR BRENDA; 3.6.1.62; 3474.
DR BRENDA; 3.6.1.64; 3474.
DR Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR BioGRID-ORCS; 75686; 2 hits in 108 CRISPR screens.
DR PRO; PR:Q6P3D0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P3D0; protein.
DR Bgee; ENSMUSG00000032565; Expressed in vestibular membrane of cochlear duct and 217 other tissues.
DR ExpressionAtlas; Q6P3D0; baseline and differential.
DR Genevisible; Q6P3D0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR GO; GO:0050897; F:cobalt ion binding; ISS:UniProtKB.
DR GO; GO:0097383; F:dIDP diphosphatase activity; IEA:RHEA.
DR GO; GO:0035870; F:dITP diphosphatase activity; IMP:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990003; F:inosine-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:1901641; F:ITP binding; ISS:UniProtKB.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
DR GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0110152; F:RNA NAD-cap (NAD-forming) hydrolase activity; IEA:RHEA.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:1901640; F:XTP binding; ISS:UniProtKB.
DR GO; GO:0006382; P:adenosine to inosine editing; ISS:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IGI:MGI.
DR GO; GO:0035863; P:dITP catabolic process; IGI:MGI.
DR GO; GO:0046709; P:IDP catabolic process; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0110155; P:NAD-cap decapping; ISS:UniProtKB.
DR GO; GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0090068; P:positive regulation of cell cycle process; ISS:UniProtKB.
DR GO; GO:0016077; P:sno(s)RNA catabolic process; ISS:UniProtKB.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..195
FT /note="U8 snoRNA-decapping enzyme"
FT /id="PRO_0000057118"
FT DOMAIN 18..173
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 61..82
FT /note="Nudix box"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6TEC1"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT CONFLICT 193
FT /note="D -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21825 MW; F0016662C97B37F1 CRC64;
MEGHRKVELS EALALGPDWR HACHALLYAP DPRKLFGRIP MRFAVLMQMR FDGRLGFPGG
FVDAQDSCLE DGLNRELREE LGEAMSAFRV ERSDYRSSHI AARPRVVAHF YAKRLTLEQL
QAVEARAPQA KDHGLEVLGL VRVPLYVLRD GEGGLPAFLE NSFIGAAREQ LLEALQDLKL
LDPGIIAKLK IPDSK
