ID A0A1B9G8R2_9TREE Unreviewed; 712 AA.
AC A0A1B9G8R2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
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=I302_02211 {ECO:0000313|EMBL:OCF27370.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF27370.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF27370.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF27370.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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; KI894019; OCF27370.1; -; Genomic_DNA.
DR RefSeq; XP_019048440.1; XM_019188878.1.
DR AlphaFoldDB; A0A1B9G8R2; -.
DR STRING; 1296100.A0A1B9G8R2; -.
DR GeneID; 30206610; -.
DR VEuPathDB; FungiDB:I302_02211; -.
DR OrthoDB; 3030505at2759; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000092730; 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:UP000092730}.
FT DOMAIN 3..273
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 712 AA; 79398 MW; BE49D68B5B97CF96 CRC64;
MHLVTVATQL DQWSLDFEGN CKRILKSIAI AKSRGATLRV GPELEIPGYG CLDHFLEGDT
ILHSWEVLAT ILQSEEAQGI VCDIGMPIEH KNNNYNCRVI IHSGKIVMIR PKMWMANDGN
YRELRHFTPW HKHRQVEQHS LPRIIRNVTG QDLVPFGDAV VSTEDTVIGV ELCEELFTPA
SPHILMGLDG VEIFTNSSAS HHELRKLNRR IDLIKEATMK LGGIYLYANQ QGCDGDRLYY
DGAALIAMNG QILARGSQFS LSDVEVITAT VDLGAVRAHR TTSSRRMQSA QAEAYQRVYV
DTRLDGGQGI RVGDEETKGS MEVIYHTPEE EIALGPACWL WDYLRRSRCQ GYFIPLSGGI
DSCATTVIIH SMCRLVADAA SKGDEQVIAD ARRIAGEPED SSYLPIDPKE FAGRIFHTCY
MGTEHSSPET RKRAKDLSEA VGGYHVDLNM DTAVSAVKGI FSLVTGKKPQ FAVHGGSSAE
NLALQNIQAR LRMVLAYMFA QLLPWARGKV GGLLVLGSAN VDESLRGYYT KYDCSSADVN
PIGGISKTDL KKFIAWAEVN FDLPILRSFL DAIPTAELIP IGSDNVAQSD EVEMGMTYDE
LSVYGRLRKV EKCGPYSMFG KLVQEWGSFL SPVEIATKVK HFFFNYAINR HKMTTLTPSV
HMESYSPDDN RFDLRPFLLP TRFNHQFRRI DELADKLPNR ATQPGNDKAK VD
//
