NADE_SALTY
ID NADE_SALTY Reviewed; 275 AA.
AC Q8ZPU5;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193};
DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193};
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193}; OrderedLocusNames=STM1310;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2] {ECO:0007744|PDB:3HMQ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NAD.
RC STRAIN=LT2;
RA Halavaty A.S., Wawrzak Z., Skarina T., Onopriyenko O., Peterson S.N.,
RA Savchenko A., Anderson W.F.;
RT "1.9 Angstrom resolution crystal structure of a NAD synthetase (nadE) from
RT Salmonella typhimurium LT2 in complex with NAD(+).";
RL Submitted (MAY-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00193};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193}.
CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
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DR EMBL; AE006468; AAL20235.1; -; Genomic_DNA.
DR RefSeq; NP_460276.1; NC_003197.2.
DR RefSeq; WP_000174981.1; NC_003197.2.
DR PDB; 3HMQ; X-ray; 1.90 A; A=1-275.
DR PDBsum; 3HMQ; -.
DR AlphaFoldDB; Q8ZPU5; -.
DR SMR; Q8ZPU5; -.
DR STRING; 99287.STM1310; -.
DR PaxDb; Q8ZPU5; -.
DR EnsemblBacteria; AAL20235; AAL20235; STM1310.
DR GeneID; 1252828; -.
DR KEGG; stm:STM1310; -.
DR PATRIC; fig|99287.12.peg.1392; -.
DR HOGENOM; CLU_059327_3_0_6; -.
DR OMA; MAFLYDY; -.
DR PhylomeDB; Q8ZPU5; -.
DR BioCyc; SENT99287:STM1310-MON; -.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; Q8ZPU5; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding; NAD;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..275
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152191"
FT BINDING 33
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 140
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 173
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 180
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|Ref.2"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 260..261
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:3HMQ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 51..71
FT /evidence="ECO:0007829|PDB:3HMQ"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3HMQ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:3HMQ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 131..152
FT /evidence="ECO:0007829|PDB:3HMQ"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3HMQ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3HMQ"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:3HMQ"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:3HMQ"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:3HMQ"
SQ SEQUENCE 275 AA; 30484 MW; 6E0F3AB5B812B6EE CRC64;
MTLQQEIIQA LGAKPHINPE EEIRRSVDFL KAYLKTYPFL KSLVLGISGG QDSTLAGKLS
QMAIAELREE TGDNALQFIA VRLPYGVQAD EQDCQDAIAF IQPDRVLTVN IKGAVLASEQ
ALREAGIELS DFVRGNEKAR ERMKAQYSIA GMTHGVVVGT DHAAEAITGF FTKYGDGGTD
INPLHRLNKR QGKQLLAALG CPEHLYKKVP TADLEDDRPS LPDEAALGVT YDNIDDYLEG
KTLDPAIAKT IEGWYVKTEH KRRLPITVFD DFWKR
