ID A0A1Q7LZI5_9CREN Unreviewed; 175 AA.
AC A0A1Q7LZI5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00243};
DE EC=2.7.7.1 {ECO:0000256|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00243};
DE AltName: Full=NMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00243};
GN ORFNames=AUJ07_00550 {ECO:0000313|EMBL:OLD05838.1};
OS Crenarchaeota archaeon 13_1_40CM_3_53_5.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805098 {ECO:0000313|EMBL:OLD05838.1, ECO:0000313|Proteomes:UP000186658};
RN [1] {ECO:0000313|EMBL:OLD05838.1, ECO:0000313|Proteomes:UP000186658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00243};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00243}.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010124, ECO:0000256|HAMAP-Rule:MF_00243}.
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:OLD05838.1}.
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DR EMBL; MNGL01000003; OLD05838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7LZI5; -.
DR STRING; 1805098.AUJ07_00550; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000186658; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00243; NMN_adenylyltr; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR006418; NMN_Atrans_arc.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR01527; arch_NMN_Atrans; 1.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR21342:SF0; BIFUNCTIONAL NMN ADENYLYLTRANSFERASE_NUDIX HYDROLASE; 1.
DR PANTHER; PTHR21342; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00243};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00243};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00243};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00243};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00243};
KW Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00243};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00243}.
FT DOMAIN 5..136
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 175 AA; 19905 MW; 522B88AA078C6964 CRC64;
MKTGLYIGRF QPFHLGHLEA VNHILKQVDE LIIVVGSAQN SHTVENPFTA GERTTMIRMA
LKDAKIEPSK YVVTPLPDAE FHVVWVAHLL SQTPAFQVAF TNEPLTARLL KEAGVHVERI
PFFQREFFTA TEVRRRMLSS EDWESLLPHA VAEYLKSIEG VERIREISLS DKTPT
//
