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Database: UniProt
Entry: C9LHY6_9BACT
LinkDB: C9LHY6_9BACT
Original site: C9LHY6_9BACT 
ID   C9LHY6_9BACT            Unreviewed;       190 AA.
AC   C9LHY6;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   ECO:0000313|EMBL:EEX71102.1};
GN   ORFNames=GCWU000325_01840 {ECO:0000313|EMBL:EEX71102.1};
OS   Alloprevotella tannerae ATCC 51259.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Alloprevotella.
OX   NCBI_TaxID=626522 {ECO:0000313|EMBL:EEX71102.1, ECO:0000313|Proteomes:UP000003460};
RN   [1] {ECO:0000313|EMBL:EEX71102.1, ECO:0000313|Proteomes:UP000003460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51259 {ECO:0000313|EMBL:EEX71102.1,
RC   ECO:0000313|Proteomes:UP000003460};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-
CC       Rule:MF_00244}.
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:EEX71102.1}.
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DR   EMBL; ACIJ02000022; EEX71102.1; -; Genomic_DNA.
DR   RefSeq; WP_006255621.1; NZ_GG700643.1.
DR   AlphaFoldDB; C9LHY6; -.
DR   STRING; 626522.GCWU000325_01840; -.
DR   GeneID; 84576648; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_069765_3_3_10; -.
DR   OrthoDB; 5295945at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000003460; Unassembled WGS sequence.
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; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1.
DR   PANTHER; PTHR39321; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR39321:SF3; 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_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:EEX71102.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_00244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003460};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:EEX71102.1}.
FT   DOMAIN          6..164
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   190 AA;  21693 MW;  AF2473B145F9B9BF CRC64;
     MKRIGIFGGS FNPIHKGHIH IGLKAIADKE VDEIHYLVSP QNPLKCDQQL LDEQLRFSLT
     IKALADYPLL KASDFEFHLP RPSFTWKTMD ALRQHYPADQ LVLLIGADNW LLFDRWANHD
     QLLANYQFLI YPRDGYEVTA TDLPANVRLL DAPIYPYSST MIRQAVQTGG DIAEMVPDAI
     KDDVKRLYGV
//
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