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Database: UniProt
Entry: H5SEB8_9GAMM
LinkDB: H5SEB8_9GAMM
Original site: H5SEB8_9GAMM 
ID   H5SEB8_9GAMM            Unreviewed;       213 AA.
AC   H5SEB8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE            EC=2.7.7.18 {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE            Short=NaMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
GN   Name=nadD {ECO:0000256|HAMAP-Rule:MF_00244};
GN   ORFNames=HGMM_F01C09C34 {ECO:0000313|EMBL:BAL52440.1}, HGMM_F16E07C11
GN   {ECO:0000313|EMBL:BAL54504.1};
OS   uncultured Gammaproteobacteria bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; environmental samples.
OX   NCBI_TaxID=86473 {ECO:0000313|EMBL:BAL54504.1};
RN   [1] {ECO:0000313|EMBL:BAL54504.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA   Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA   Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT   "Genetic and functional properties of uncultivated thermophilic
RT   crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT   genome fragments.";
RL   Environ. Microbiol. 7:1967-1984(2005).
RN   [2] {ECO:0000313|EMBL:BAL54504.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA   Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT   "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT   Pathway Dominates a Subsurface Ecosystem.";
RL   PLoS ONE 7:e30559-e30559(2012).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000256|ARBA:ARBA00002324, ECO:0000256|HAMAP-Rule:MF_00244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC         + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58437; EC=2.7.7.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00001785, ECO:0000256|HAMAP-
CC         Rule:MF_00244};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005019, ECO:0000256|HAMAP-Rule:MF_00244}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000256|ARBA:ARBA00009014,
CC       ECO:0000256|HAMAP-Rule:MF_00244}.
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DR   EMBL; AP011628; BAL52440.1; -; Genomic_DNA.
DR   EMBL; AP011691; BAL54504.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5SEB8; -.
DR   UniPathway; UPA00253; UER00332.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02165; NMNAT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00244; NaMN_adenylyltr; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1.
DR   PANTHER; PTHR39321; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR39321:SF3; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00244};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00244};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000313|EMBL:BAL54504.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_00244};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:BAL54504.1}.
FT   DOMAIN          4..179
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   213 AA;  24345 MW;  38D511A346074539 CRC64;
     MIGILGGTFD PIHYGHLRTA LEVKEALGLE AVRFIPARQP PHRAPPLASP EARRRMLEVA
     LADAPPEFVL DTRELKRPGP SYMVDTLKSL RQELGQIPLC LILGMDAFLG LTTWHRWQQI
     FELAHVIVMT RPGYALRWPA EWMQGRQVRE KQVLRCQPAG NLYFQPVIQL EISSSFIRRC
     LAIGRDPKYL LPESVLALIR QEGYYQLPQS VEK
//
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