ID F2U6F5_SALR5 Unreviewed; 708 AA.
AC F2U6F5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|PIRNR:PIRNR006630};
DE EC=6.3.5.1 {ECO:0000256|PIRNR:PIRNR006630};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|PIRNR:PIRNR006630};
GN ORFNames=PTSG_03736 {ECO:0000313|EMBL:EGD83096.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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|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|PIRNR:PIRNR006630}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000256|ARBA:ARBA00007145, ECO:0000256|PIRNR:PIRNR006630}.
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DR EMBL; GL832962; EGD83096.1; -; Genomic_DNA.
DR RefSeq; XP_004995460.1; XM_004995403.1.
DR AlphaFoldDB; F2U6F5; -.
DR STRING; 946362.F2U6F5; -.
DR EnsemblProtists; EGD83096; EGD83096; PTSG_03736.
DR GeneID; 16076041; -.
DR KEGG; sre:PTSG_03736; -.
DR eggNOG; KOG2303; Eukaryota.
DR InParanoid; F2U6F5; -.
DR OMA; TSQEVCN; -.
DR OrthoDB; 3030505at2759; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000007799; 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: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; 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|PIRNR:PIRNR006630};
KW Ligase {ECO:0000256|PIRNR:PIRNR006630};
KW NAD {ECO:0000256|PIRNR:PIRNR006630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR006630};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799}.
FT DOMAIN 4..274
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 708 AA; 79763 MW; 0E821D30A150DCD3 CRC64;
MSLITVATCS LNQWALDFEG NYERILESIR ESKKRGAVLR VGPELEISGY GCNDHFYEPD
TFYHSYQMLA KLIAHEDCQD IVVDVGLPMM HKSVRYNCRI IFFNGKVLLI RPKMYLAMNG
NYREGRWFTP WRRHRTLEDF NLPAVVRKVT GQLSVPFGDG VISANDVTIG SEICEELWSP
NSPHIHMGLD GIDIFTNGSG SHHELRKLDY RLNLMRDATA KSGGVYLYAN SQGNDGERVY
YDGCALIVLN GKILAQGSQF SLRDVEVLTA TIDLEDIRTY RGSLISLADQ AAVSNAYPRI
QTGHDMCMEH GSARPTRPIE PFLHTPEQEI ALGPACWLWD YLRRSGLGGF FLPLSGGMDS
SSTASIVCSM CHLVVEAIEN GNEQVLADVR RIVRDEEFVP STPQEIAAKI FFTMYMGTTN
SSKETRDRAK GLANEIGAVH YDINMDTAVS AITSLFALVT GKTPKFKVHG GSHQENLALQ
NIQARLRMVL SYLFGSLLPW CHGRHGSLLV LGSANVDECL RGYMTKYDCS SADLNPIGGI
SKADLRRFLP FAAERFKLPS LHGILSAKPT AELEPITEGY TQTDEEDMGM TYDELSTYGR
LRKISKCGPY SMFRKLVDLW SDRLTVRQIA DKVKYFFRMY SINRHKTTVL TPSYHAEGYS
PDDNRFDLRP FLYNTRWTLP FKCIDNDVSR CEEAVHHREE AACQEPTA
//
