NADE_PSEAE
ID NADE_PSEAE Reviewed; 275 AA.
AC Q9HUP3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PA4920;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:4XFD}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Dranow D.M., Lorimer D., Edwards T.E.;
RT "Crystal structure of a NH(3)-dependent NAD(+) synthetase from Pseudomonas
RT aeruginosa.";
RL Submitted (DEC-2014) to the PDB data bank.
RN [3] {ECO:0007744|PDB:5F23}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NAD.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Abendroth J., Mayclin S.J., Lorimer D.D., Edwards T.E.;
RT "Crystal structure of NH(3)-dependent NAD(+) synthetase Pseudomonas
RT aeruginosa in complex with NAD.";
RL Submitted (DEC-2015) 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; AE004091; AAG08305.1; -; Genomic_DNA.
DR PIR; F83030; F83030.
DR RefSeq; NP_253607.1; NC_002516.2.
DR RefSeq; WP_003099998.1; NZ_QZGE01000002.1.
DR PDB; 4XFD; X-ray; 1.55 A; A=1-275.
DR PDB; 5F23; X-ray; 1.50 A; A=1-275.
DR PDBsum; 4XFD; -.
DR PDBsum; 5F23; -.
DR AlphaFoldDB; Q9HUP3; -.
DR SMR; Q9HUP3; -.
DR STRING; 287.DR97_2271; -.
DR PaxDb; Q9HUP3; -.
DR PRIDE; Q9HUP3; -.
DR DNASU; 882213; -.
DR EnsemblBacteria; AAG08305; AAG08305; PA4920.
DR GeneID; 882213; -.
DR KEGG; pae:PA4920; -.
DR PATRIC; fig|208964.12.peg.5153; -.
DR PseudoCAP; PA4920; -.
DR HOGENOM; CLU_059327_3_0_6; -.
DR InParanoid; Q9HUP3; -.
DR OMA; MAFLYDY; -.
DR PhylomeDB; Q9HUP3; -.
DR BioCyc; PAER208964:G1FZ6-5034-MON; -.
DR UniPathway; UPA00253; UER00333.
DR Proteomes; UP000002438; 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_0000152185"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 143
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 147
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|Ref.3"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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.3"
FT BINDING 187
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 267..268
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|Ref.3"
FT BINDING 268
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000305|Ref.3"
FT HELIX 1..11
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 21..42
FT /evidence="ECO:0007829|PDB:5F23"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 55..75
FT /evidence="ECO:0007829|PDB:5F23"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:5F23"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 134..160
FT /evidence="ECO:0007829|PDB:5F23"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:5F23"
FT TURN 180..184
FT /evidence="ECO:0007829|PDB:5F23"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:5F23"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:5F23"
SQ SEQUENCE 275 AA; 29697 MW; 4CD3AE92F3FC2146 CRC64;
MQQIQRDIAQ ALQVQPPFQS EADVQAQIAR RIAFIQQCLK DSGLKTLVLG ISGGVDSLTA
GLLAQRAVEQ LREQTGDQAY RFIAVRLPYQ VQQDEADAQA SLATIRADEE QTVNIGPSVK
ALAEQLEALE GLEPAKSDFV IGNIKARIRM VAQYAIAGAR GGLVIGTDHA AEAVMGFFTK
FGDGACDLAP LSGLAKHQVR ALARALGAPE NLVEKIPTAD LEDLRPGHPD EASHGVTYAE
IDAFLHGQPL REEAARVIVD TYHKTQHKRE LPKAP
