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Entry: A0A095VQS7_9GAMM
LinkDB: A0A095VQS7_9GAMM
Original site: A0A095VQS7_9GAMM 
ID   A0A095VQS7_9GAMM        Unreviewed;       543 AA.
AC   A0A095VQS7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
DE            EC=6.3.5.1 {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
GN   Name=nadE {ECO:0000256|HAMAP-Rule:MF_02090};
GN   ORFNames=HRUBRA_01657 {ECO:0000313|EMBL:KGE03720.1};
OS   Pseudohaliea rubra DSM 19751.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Pseudohaliea.
OX   NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE03720.1, ECO:0000313|Proteomes:UP000029640};
RN   [1] {ECO:0000313|EMBL:KGE03720.1, ECO:0000313|Proteomes:UP000029640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE03720.1,
RC   ECO:0000313|Proteomes:UP000029640};
RX   PubMed=25414506;
RA   Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT   "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT   19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL   Genome Announc. 2:e01208-14(2014).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC       NAD. Uses L-glutamine as a nitrogen source. {ECO:0000256|HAMAP-
CC       Rule:MF_02090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate +
CC         H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.5.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02090,
CC         ECO:0000256|PIRNR:PIRNR006630};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000256|ARBA:ARBA00005188,
CC       ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family.
CC       {ECO:0000256|RuleBase:RU003811}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC       family. {ECO:0000256|ARBA:ARBA00007145, ECO:0000256|HAMAP-
CC       Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02090}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGE03720.1}.
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DR   EMBL; AUVB01000050; KGE03720.1; -; Genomic_DNA.
DR   RefSeq; WP_035517061.1; NZ_KN234774.1.
DR   AlphaFoldDB; A0A095VQS7; -.
DR   STRING; 1265313.HRUBRA_01657; -.
DR   PATRIC; fig|1265313.6.peg.1638; -.
DR   eggNOG; COG0171; Bacteria.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_022313_2_0_6; -.
DR   OrthoDB; 9760188at2; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000029640; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07570; GAT_Gln-NAD-synth; 1.
DR   CDD; cd00553; NAD_synthase; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_02090; NadE_glutamine_dep; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR014445; Gln-dep_NAD_synthase.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR003694; NAD_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00552; nadE; 1.
DR   PANTHER; PTHR23090:SF9; GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE; 1.
DR   PANTHER; PTHR23090; NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PIRSF; PIRSF006630; NADS_GAT; 2.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02090}; Glutamine amidotransferase {ECO:0000313|EMBL:KGE03720.1};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02090}; Reference proteome {ECO:0000313|Proteomes:UP000029640};
KW   Transferase {ECO:0000313|EMBL:KGE03720.1}.
FT   DOMAIN          4..247
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   ACT_SITE        45
FT                   /note="Proton acceptor; for glutaminase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   ACT_SITE        113
FT                   /note="For glutaminase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   ACT_SITE        149
FT                   /note="Nucleophile; for glutaminase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         119
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         175
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         181
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         290..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         373
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         402
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT   BINDING         512
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
SQ   SEQUENCE   543 AA;  58875 MW;  87C57EC979ED5900 CRC64;
     MAKLDILMAQ LNTRVGDFEG NADRVLAVAR RAVGERSAPV IVFPELTLSG YPPEDLLLRP
     SLEGRVQRTL ARLRRELPAE AVVVLGYPRR RDGNLYNMAG VLTGGALVAE YAKRCLPNYQ
     VFDEKRYFSG GDAAQLLEIA GVPVALSVCE DIWDEAPILD SAAAGAKLLL NLNASPFHRG
     KQRERREVVG ARARTAGLPV VYVNQVGGQD ELVFDGGSFA VDANGEVMAS APHFREAECW
     VSVEVDDGGP VRLGGTQVAP PEDLAATWEA LVLGVRDYVD KNGFPGVVLG LSGGVDSALT
     LAVAVEALGA DRVEAVMMPF RYTSSMSVED AAEQSRLLGV RHSVISIEGA YNAFMQALAP
     HFEGLAPDTT EENLQARCRG VLLMSLSNKG GALVLTTGNK SELAVGYSTL YGDMAGGFDV
     LKDVPKTLVY ALCRYRNSLG PCIPERVIDR PPSAELAPDQ RDDDSLPAYP VLDDILERYV
     EQDESAEAII AAGLPREQVE RVVRLVDRNE YKRRQAPIGV RITRRGFGRD RRYPITSAWL
     PGD
//
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