ID K1M700_9FLAO Unreviewed; 194 AA.
AC K1M700;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=HMPREF9699_00623 {ECO:0000313|EMBL:EKB58133.1};
OS Bergeyella zoohelcum ATCC 43767.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Bergeyella.
OX NCBI_TaxID=883096 {ECO:0000313|EMBL:EKB58133.1, ECO:0000313|Proteomes:UP000006085};
RN [1] {ECO:0000313|EMBL:EKB58133.1, ECO:0000313|Proteomes:UP000006085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43767 {ECO:0000313|EMBL:EKB58133.1,
RC ECO:0000313|Proteomes:UP000006085};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bergeyella zoohelcum ATCC 43767.";
RL Submitted (JUL-2012) 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:EKB58133.1}.
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DR EMBL; AGYA01000016; EKB58133.1; -; Genomic_DNA.
DR RefSeq; WP_002662344.1; NZ_JH932293.1.
DR AlphaFoldDB; K1M700; -.
DR STRING; 883096.HMPREF9699_00623; -.
DR PATRIC; fig|883096.3.peg.635; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_3_3_10; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000006085; 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; 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; 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:EKB58133.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000006085};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:EKB58133.1}.
FT DOMAIN 6..167
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 194 AA; 22432 MW; 3C3C3482CD0FB254 CRC64;
MKQIGLFFGS FNPIHIGHII LANHILEFSN LDEIWFVVTP HNPFKEKKTL LNDQNRLYMV
ELALKNYPNM KASNIEFSLP QPSYTIDTLA YLKERHPSYT FSLIMGEDNL SGLQKWKNAD
VLIAHYPIYV YPRLTETTSA GKKLLELPTI QKIDAPIIEL SATQIRNMIK ENKNVRPMLP
PEVFDYLDGS SFYK
//
