ID R5YH12_9FIRM Unreviewed; 635 AA.
AC R5YH12;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=BN528_00690 {ECO:0000313|EMBL:CDA26200.1};
OS Roseburia sp. CAG:197.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262943 {ECO:0000313|EMBL:CDA26200.1, ECO:0000313|Proteomes:UP000018336};
RN [1] {ECO:0000313|EMBL:CDA26200.1, ECO:0000313|Proteomes:UP000018336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:197 {ECO:0000313|Proteomes:UP000018336};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDA26200.1}.
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DR EMBL; CBBL010000301; CDA26200.1; -; Genomic_DNA.
DR AlphaFoldDB; R5YH12; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000018336; 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:UP000018336}.
FT DOMAIN 6..269
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT ACT_SITE 46
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 115
FT /note="For glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT ACT_SITE 171
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 121
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 198
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 204
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 348..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 434
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 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090"
FT BINDING 463
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 468..471
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 595
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 635 AA; 70394 MW; A5110CB4E84D2F77 CRC64;
MKQGFVKVAA VTPKIKVADT AYNGKLICSY MEECAKEGAK IVVFPELCIT GYTCQDLFLQ
DKLLQGAEEE LLQIAECSAS MDGIFFVGLP YEVNGKLYNM AAVISGGEVL GMVPKSFLPN
YNEFYERRHF TPGAELCTEV TLSDGSVVPV DRDLLFTCDS MRRLRIGVEL CEDLWTPNPP
SIGHALAGAT VIVNLSASNE ITGKDSYRRE LVAGQSARLL SAYIYASAGE GESTQDLVFS
GHNIIAENGH ILAESKRFTY GVVYSEIDVE KLTEERRRMT TFEIEDTHTD IAFSLKTEET
KLTRFVDPAP FVPGDKNTRE KRCDEILMIQ AMGLKKRLEH TNANAVVGIS GGLDSTLALL
VTARAFDLSG KDRKGIIAVT MPGFGTTDRT YDNAVKLIEC LGATFVEVDI KNAVNIHFSD
IGQDPAVHDV TYENSQARER TQILMDIANK NNALVIGTGD LSELALGWAT YNGDHMSMYA
VNASVPKTLV RHLVRYYADT CQDRELEKTL LDVLDTPVSP ELLPPEDGKI SQKTEDLVGP
YELHDFFLYH MLRLGFSPAK IYRLARIAFA GTYEDDFILK WLKTFYHRFF AQQFKRSCLP
DGPKVGSVAV SPRGDLRMPS DACATLWKSE LETLG
//
