ID A0A023D8U6_ACIMT Unreviewed; 677 AA.
AC A0A023D8U6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=Amme_172_022 {ECO:0000313|EMBL:GAJ30553.1};
OS Acidomonas methanolica NBRC 104435.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidomonas.
OX NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ30553.1, ECO:0000313|Proteomes:UP000019760};
RN [1] {ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
RN [2] {ECO:0000313|EMBL:GAJ30553.1, ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|EMBL:GAJ30553.1,
RC ECO:0000313|Proteomes:UP000019760};
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(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: 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:GAJ30553.1}.
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DR EMBL; BAND01000164; GAJ30553.1; -; Genomic_DNA.
DR RefSeq; WP_042061797.1; NZ_BJVB01000035.1.
DR AlphaFoldDB; A0A023D8U6; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000019760; 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:UP000019760}.
FT DOMAIN 14..279
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 179
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 206
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 212
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 457
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 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 486
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 491..494
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 634
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 677 AA; 73365 MW; F8815BA1B5137B73 CRC64;
MTADFHNPYR HGFARIAACT LPVRLADPAA NAAALSVEAA ACSAEHVAIA VFPELCLSGY
ALDDLRQQDA LLDAVERALH TLAEASRAWS CVAVIGAPLR HADRLFNCAV LLHRGRILGI
VPKSYLPNYR EFYEARQFAP GVTRRNETLT LGDMSIPFGT DLLFTAEDVP GLTLGVEICE
DLWVPTPPST ALAMAGASII ANPSASNITI GKAEDRTLLI RSQSLRALCA YAYAAAGPGE
STTDVAWDGQ VSLHEVGTLL AESPRFPRAA ARAVADIDLD LIRQERSRMG SFAACADAQP
PLVWRRIPFR VAPPAAAIPL RRTVPRFPFV PADPGRLAQD CYEGWTIQVS ALIQRLSASG
VRRMVIGVSG GLDSTLALLV CARAADELGW PRTAVAAYTM PGFATGATSL AFARRLMSGL
GVSAHELDIR PTARQMLETI GHPFAKGEAV HDVTFENVQA GLRTDFLFRL ANQLNGLVIG
TGDLSELALG WCTYGVGDQM AHYNVNAGMP KTLIQHLIRW LAREGDWAEA VGPLLDEIVS
AEISPELVPG DHPQSTEAKI GPYALQDFNL FHTLRYGFRP AKIAYLALHA WSDAARGAWP
ANFPEDRRVA YDLPAIRHWL EVFLRRFFAF SQFKRSAMPN GPKLTPGGGL SPRGDWRAPS
DSTAVAWLED LETVPKS
//
