NADM_SYNY3
ID NADM_SYNY3 Reviewed; 339 AA.
AC Q55928;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Bifunctional NMN adenylyltransferase/Nudix hydrolase;
DE Includes:
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase;
DE EC=2.7.7.1;
DE AltName: Full=NAD(+) diphosphorylase;
DE AltName: Full=NAD(+) pyrophosphorylase;
DE AltName: Full=NMN adenylyltransferase;
DE Includes:
DE RecName: Full=ADP compounds hydrolase;
DE EC=3.6.1.-;
GN OrderedLocusNames=slr0787;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10050763; DOI=10.1016/s0014-5793(99)00068-x;
RA Raffaelli N., Lorenzi T., Amici A., Emanuelli M., Ruggieri S., Magni G.;
RT "Synechocystis sp. slr0787 protein is a novel bifunctional enzyme endowed
RT with both nicotinamide mononucleotide adenylyltransferase and 'Nudix'
RT hydrolase activities.";
RL FEBS Lett. 444:222-226(1999).
CC -!- FUNCTION: The Nudix hydrolase domain is active on ADP-ribose, (2')-
CC phospho-ADP-ribose, IDP-ribose and NADPH.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC -!- INTERACTION:
CC Q55928; Q55928: slr0787; NbExp=2; IntAct=EBI-1622828, EBI-1622828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the archaeal NMN
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10693.1; -; Genomic_DNA.
DR PIR; S77001; S77001.
DR PDB; 2QJO; X-ray; 2.60 A; A/B/C=1-339.
DR PDBsum; 2QJO; -.
DR AlphaFoldDB; Q55928; -.
DR SMR; Q55928; -.
DR DIP; DIP-29582N; -.
DR IntAct; Q55928; 3.
DR STRING; 1148.1001812; -.
DR PaxDb; Q55928; -.
DR EnsemblBacteria; BAA10693; BAA10693; BAA10693.
DR KEGG; syn:slr0787; -.
DR eggNOG; COG1051; Bacteria.
DR eggNOG; COG1056; Bacteria.
DR InParanoid; Q55928; -.
DR OMA; YPPVFVT; -.
DR PhylomeDB; Q55928; -.
DR BioCyc; MetaCyc:MON-8321; -.
DR BRENDA; 2.7.7.1; 382.
DR BRENDA; 3.6.1.13; 382.
DR UniPathway; UPA00253; UER00600.
DR EvolutionaryTrace; Q55928; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02168; NMNAT_Nudix; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR041750; NMNAT_Nudix.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW Multifunctional enzyme; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..339
FT /note="Bifunctional NMN adenylyltransferase/Nudix
FT hydrolase"
FT /id="PRO_0000135011"
FT DOMAIN 199..335
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 1..183
FT /note="NMN adenylyltransferase"
FT MOTIF 233..254
FT /note="Nudix box"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 32..42
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2QJO"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 173..190
FT /evidence="ECO:0007829|PDB:2QJO"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2QJO"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2QJO"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:2QJO"
SQ SEQUENCE 339 AA; 38532 MW; B12938EBE97465BB CRC64;
MQTKYQYGIY IGRFQPFHLG HLRTLNLALE KAEQVIIILG SHRVAADTRN PWRSPERMAM
IEACLSPQIL KRVHFLTVRD WLYSDNLWLA AVQQQVLKIT GGSNSVVVLG HRKDASSYYL
NLFPQWDYLE TGHYPDFSST AIRGAYFEGK EGDYLDKVPP AIADYLQTFQ KSERYIALCD
EYQFLQAYKQ AWATAPYAPT FITTDAVVVQ AGHVLMVRRQ AKPGLGLIAL PGGFIKQNET
LVEGMLRELK EETRLKVPLP VLRGSIVDSH VFDAPGRSLR GRTITHAYFI QLPGGELPAV
KGGDDAQKAW WMSLADLYAQ EEQIYEDHFQ IIQHFVSKV
