ID A0A0F0CR71_9BACT Unreviewed; 424 AA.
AC A0A0F0CR71;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=OMAG_000314 {ECO:0000313|EMBL:KJJ85818.1};
OS Candidatus Omnitrophus magneticus.
OC Bacteria; Candidatus Omnitrophota; Omnitrophus.
OX NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ85818.1, ECO:0000313|Proteomes:UP000033428};
RN [1] {ECO:0000313|EMBL:KJJ85818.1, ECO:0000313|Proteomes:UP000033428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ85818.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) 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: 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|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:KJJ85818.1}.
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DR EMBL; JYNY01000068; KJJ85818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0CR71; -.
DR PATRIC; fig|1609969.3.peg.349; -.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000033428; 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; cd00553; NAD_synthase; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR Gene3D; 3.40.50.620; HUPs; 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, ECO:0000256|RuleBase:RU003811};
KW NAD {ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR006630};
KW Reference proteome {ECO:0000313|Proteomes:UP000033428}.
FT DOMAIN 1..87
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 47039 MW; 1062541A5D9A89CC CRC64;
MAQAAGGADI IFNISASPYH AGKSKERVDL ARDRARETNA VIVYANLIGG QDELVFDGAS
FIVDPRGEII AGGKHFEEDL VIADINLDKF KKAPVVQKKQ NTLKRIYIFP ALKQEKINLV
KKKFIENSNI QQGNVNSLTK KMGNIEEIYR ALVLGTKDYV IKNGFKKIIL GLSGGIDSAL
TAVIACEALG KENVIGVTMP SPYSSSETFN DAKKIAQNLE IMFYEVPIET AMNAYKEILA
PVFKDGARGI VEENLQARIR GNILMAFSNN YGWLVLTTGN KSETAVGYST LYGDTAGGFA
VIKDVPKTVV YELSNFINKQ TNRELIPKTI IKRAPSAELR PNQKDTDSLP EYNILDQILK
LYIEEDKSII DIQKTGAGKT VIKNIINLVD KSEYKRRQSP PGIRITPKSF GKDRRLPITN
KYQE
//
