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Entry: A0A1B8G3W6_9PEZI
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ID   A0A1B8G3W6_9PEZI        Unreviewed;       718 AA.
AC   A0A1B8G3W6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=VE02_01155 {ECO:0000313|EMBL:OBT90524.1};
OS   Pseudogymnoascus sp. 03VT05.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT90524.1};
RN   [1] {ECO:0000313|EMBL:OBT90524.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03VT05 {ECO:0000313|EMBL:OBT90524.1};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) 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; KV459357; OBT90524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8G3W6; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000091872; 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   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}.
FT   DOMAIN          5..275
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   718 AA;  80577 MW;  AC5ED99FB99F1B0D CRC64;
     MGHLVTLATC SLNQWALDFE GNAQRILQSI KEAKAGGASL RIGPELEITG YGCLDHFLES
     DTDLHSWESL VMILEDPICK DILLDIGMPV MHKNVKYNAR ILSLNQEILL IRPKLSLAND
     GNYREMRYFS PWKGERIVED FYLPRSVQKL TGQKKCRIGD ALISTLDSCM SNETCEELFT
     PMSPALGAGL DGSEITLNSS GSHHELRKLN TRIDLIRQET LKSGGIYLYS NQQGCDGDRL
     YYDGCAMIII NGRIVAQGSQ FSLNDVETII ATVDIEEVRS YRSQKSRALQ ATKSPVYERV
     EVNFSLSSAS EEVDLRVRPS PEIAIKYHLP EEEIAYGPAC WLWDYLRRSS SGGFFLPLSG
     GVDSCATAVC RLVYQAVLER KNPQVIKDLL KIVGEPSDSK WLPSSPQDVA SRLFHTAYLG
     MAENSSKDTR SRAKALAKDI GAYHLDLNID TVYYAVTTLF TTVTSYAPKF KMFGGTPASN
     LALQNIQARL RMVLSYLFAQ LLPTVRGRNK NNPENQNPGA LLVLGSANVD ESLRGYLTKY
     DCSSADINPI GGIAKQDLKR FILWAATNFD LPILPDFIAA PPTAELEPIT ADYVQSDEAD
     MGMTYDELSI YGRMRKVDKL GPYGMWSKLL HQWSDKLSPQ EIYTKVRWFF WNYGINRHKM
     TTLTPSYHAE QYSPDDNRFD LRPFLYPSWF GFKAIEKKLA AMGENGTKVA DAEERKSS
//
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