ID Q5NHR1_FRATT Unreviewed; 347 AA.
AC Q5NHR1; A0A0G2RNS1;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000313|EMBL:CAG45019.1};
DE EC=2.7.7.1 {ECO:0000313|EMBL:CAG45019.1};
DE EC=3.6.1.- {ECO:0000313|EMBL:CAG45019.1};
GN Name=nadM {ECO:0000313|EMBL:CAG45019.1};
GN OrderedLocusNames=FTT_0386 {ECO:0000313|EMBL:CAG45019.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45019.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG45019.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2] {ECO:0007829|PDB:2QJT, ECO:0007829|PDB:2R5W}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH AMP; MAGNESIUM AND
RP MANGANESE, AND DISULFIDE BONDS.
RX PubMed=18275811; DOI=10.1016/j.str.2007.11.017;
RA Huang N., Sorci L., Zhang X., Brautigam C.A., Li X., Raffaelli N.,
RA Magni G., Grishin N.V., Osterman A.L., Zhang H.;
RT "Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure
RT and function in bacterial NAD metabolism.";
RL Structure 16:196-209(2008).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582}.
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DR EMBL; AJ749949; CAG45019.1; -; Genomic_DNA.
DR RefSeq; WP_003020070.1; NZ_CP010290.1.
DR RefSeq; YP_169431.1; NC_006570.2.
DR PDB; 2QJT; X-ray; 2.30 A; A/B=1-347.
DR PDB; 2R5W; X-ray; 2.30 A; A/B=1-347.
DR PDBsum; 2QJT; -.
DR PDBsum; 2R5W; -.
DR AlphaFoldDB; Q5NHR1; -.
DR SMR; Q5NHR1; -.
DR IntAct; Q5NHR1; 2.
DR DNASU; 3192435; -.
DR EnsemblBacteria; CAG45019; CAG45019; FTT_0386.
DR KEGG; ftu:FTT_0386; -.
DR PATRIC; fig|177416.36.peg.475; -.
DR OrthoDB; 542521at2; -.
DR BRENDA; 2.7.7.1; 2324.
DR BRENDA; 3.6.1.13; 2324.
DR EvolutionaryTrace; Q5NHR1; -.
DR Proteomes; UP000001174; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd02168; NMNAT_Nudix; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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 NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR43736; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR43736:SF1; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2QJT, ECO:0007829|PDB:2R5W};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAG45019.1};
KW Metal-binding {ECO:0007829|PDB:2QJT, ECO:0007829|PDB:2R5W};
KW Nucleotide-binding {ECO:0007829|PDB:2QJT};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAG45019.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW Transferase {ECO:0000313|EMBL:CAG45019.1}.
FT DOMAIN 201..342
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 178
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 190
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 199
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 234
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 236
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 250
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="5"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="5"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="5"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="5"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2R5W"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="5"
FT /evidence="ECO:0007829|PDB:2QJT"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:2QJT"
FT DISULFID 270..343
FT /evidence="ECO:0007829|PDB:2QJT, ECO:0007829|PDB:2R5W"
SQ SEQUENCE 347 AA; 40409 MW; 89B7DFE3DCA89840 CRC64;
MYDISVFIGR FQPFHKGHLH NIIIALQNSK KVIINIGSCF NTPNIKNPFS FEQRKQMIES
DLQVAGIDLD TVVIEPLADY FYQEQKWQDE LRKNVYKHAK NNNSIAIVGH IKDSSSYYIR
SFPEWDYIGV DNYKNFNATE FRQKFYNGII SKQYMCSNDP KLGTYNFLTK FMDTQVYQDL
VAENNYVIEY KRLWLKAPFK PNFVTVDALV IVNDHILMVQ RKAHPGKDLW ALPGGFLECD
ETIAQAIIRE LFEETNINLT HEQLAIAKRC EKVFDYPDRS VRGRTISHVG LFVFDQWPSL
PEINAADDAK DVKWISLGSN IKNICDRMLE DHYQIITILL EECGKKL
//
