ID J3C0E7_9BURK Unreviewed; 690 AA.
AC J3C0E7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=PMI40_04775 {ECO:0000313|EMBL:EJM95963.1};
OS Herbaspirillum sp. YR522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJM95963.1, ECO:0000313|Proteomes:UP000007507};
RN [1] {ECO:0000313|EMBL:EJM95963.1, ECO:0000313|Proteomes:UP000007507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR522 {ECO:0000313|EMBL:EJM95963.1,
RC ECO:0000313|Proteomes:UP000007507};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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: 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:EJM95963.1}.
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DR EMBL; AKJA01000155; EJM95963.1; -; Genomic_DNA.
DR RefSeq; WP_008119880.1; NZ_AKJA01000155.1.
DR AlphaFoldDB; J3C0E7; -.
DR STRING; 1144342.PMI40_04775; -.
DR PATRIC; fig|1144342.3.peg.4326; -.
DR eggNOG; COG0171; Bacteria.
DR eggNOG; COG0388; Bacteria.
DR OrthoDB; 8817375at2; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000007507; 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: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; 1.10.10.1140; Glutamine-dependent NAD+ synthetase, C-terminal domain; 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; IPR041856; NAD+_synth_C.
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; 1.
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};
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:UP000007507}.
FT DOMAIN 14..278
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT ACT_SITE 54
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 123
FT /note="For glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 178
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 129
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 205
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 211
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 370..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 460
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 484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 489
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 494..497
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 640
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 690 AA; 75407 MW; 09B0DEE80C400616 CRC64;
MPSEFFNLYN HGFARVAVAV PQCKVADPAF NAARTIELAR QAAAQGAVLV SFPELGLSAY
SCEDLFQQKA LLDGAQQALQ AVVEASIDLP AVLIVGLPLK IDHQLFNCAA VVANGRVHGV
VPKTYLPNYS EFYEARQFSP ADCVISSHVR LGGQDVPVGS LLFDIAGIAD FRFHVEICED
VWVPIPPSSF AALAGATVLV NLSASNVVVG KSGYRHQLVS QQSARCMAAY LYSSAGNGES
TTDVAWDGQA LICENGELLA QSERFGDGGH VIYADVDLER LSRERFHQTS FGQSVRRHAD
EVRRFDIVTI ELPAFAPAGP LPLRRQVARF PYVPASAALR EERCAEVYHI QVQALVQRLS
SSAIQKVVIG VSGGLDSTHA LLVCAKAMDK LGLPRSNILA YTMPGFATSG RTLDQAHRLM
RQVGCSAQEI DIRPSCELML KDLGHPYARG EAVYDITFEN VQAGERTNHL FRLANHNNAI
VIGTGDLSEL ALGWCTYGVG DHMSHYNVNA SVPKTLITHL VRWVAESSSL ALEDPEVLMQ
VLDTEISPEL VPGASTSAPG QRTQDFIGPY ELQDFNLYYI LRYGFTPAKV AFLAHSAWHD
SGQGHWPDGL HGTRNVYTLA QIKKNLGIFV YRFFKTSQFK RSCVPNAPKV GSGGSLSPRG
DWRAPSDSEA TLWLENLQAI PENEDQVWMR
//
