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Database: UniProt
Entry: A0A1H6FFH8_9GAMM
LinkDB: A0A1H6FFH8_9GAMM
Original site: A0A1H6FFH8_9GAMM 
ID   A0A1H6FFH8_9GAMM        Unreviewed;       421 AA.
AC   A0A1H6FFH8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000256|RuleBase:RU003812};
DE            EC=6.3.1.5 {ECO:0000256|RuleBase:RU003812};
GN   Name=nadE {ECO:0000313|EMBL:SEH08393.1};
GN   ORFNames=MBHS_04285 {ECO:0000313|EMBL:SEH08393.1};
OS   Candidatus Venteria ishoeyi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Venteria.
OX   NCBI_TaxID=1899563 {ECO:0000313|EMBL:SEH08393.1, ECO:0000313|Proteomes:UP000236724};
RN   [1] {ECO:0000313|EMBL:SEH08393.1, ECO:0000313|Proteomes:UP000236724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBHS1 {ECO:0000313|EMBL:SEH08393.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC         NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC         Evidence={ECO:0000256|RuleBase:RU003812};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004790}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family.
CC       {ECO:0000256|RuleBase:RU003811}.
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DR   EMBL; FMSV02000549; SEH08393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6FFH8; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000236724; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR037237; IlvD/EDD_N.
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; PF00920; ILVD_EDD; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003811};
KW   Ligase {ECO:0000256|RuleBase:RU003811, ECO:0000313|EMBL:SEH08393.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|RuleBase:RU003811};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003811};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236724};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..341
FT                   /note="NAD/GMP synthase"
FT                   /evidence="ECO:0000259|Pfam:PF02540"
SQ   SEQUENCE   421 AA;  47160 MW;  FF3411E6688B0804 CRC64;
     MLEQDIKPRD IMTRAAFENA MVLLMALGGS TNAVLHLIAM ARSVDVELSI DDFQAISDRI
     PFIADLKPSG RYVMEDLHNV GLYDYSAKSR SQGFALSLSG GADSAAVACL IRLMVELGVA
     EVGIENFCAR LNLPQTELNT IEQLMPVLLV CVYQATRNSS ETTRNAAEKM AHAVGAEYLE
     LDIENMVSGY RQHIEQAIGR SLNWTQDDLA LQNIQARARA PGVWMLANLR NALLLATSNR
     SEAAVGYATM DGDTSGGLSP LAGIDKHFIR HWLRWLEQNA PNSPGVNPIP ALSYINTQQP
     TAELRPGAEQ TDEADLMPYV LLNAIEKAAI RDRQTPWEIY CLLNSRFDYT AEQLLTWIER
     FFQLWIRNQW KRERYAPSFH LDDESLDPKT WCRFPILSGG FSHELKEMRK NALSQMGEEP
     G
//
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