NADD_SYNY3
ID NADD_SYNY3 Reviewed; 200 AA.
AC P73246;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase;
DE EC=2.7.7.18;
DE AltName: Full=Deamido-NAD(+) diphosphorylase;
DE AltName: Full=Deamido-NAD(+) pyrophosphorylase;
DE AltName: Full=Nicotinate mononucleotide adenylyltransferase;
DE Short=NaMN adenylyltransferase;
GN Name=nadD; OrderedLocusNames=sll1916;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17273.1; -; Genomic_DNA.
DR PIR; S75359; S75359.
DR AlphaFoldDB; P73246; -.
DR SMR; P73246; -.
DR STRING; 1148.1652350; -.
DR PaxDb; P73246; -.
DR EnsemblBacteria; BAA17273; BAA17273; BAA17273.
DR KEGG; syn:sll1916; -.
DR eggNOG; COG1057; Bacteria.
DR InParanoid; P73246; -.
DR OMA; DNPFKSH; -.
DR PhylomeDB; P73246; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR CDD; cd02165; NMNAT; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
PE 3: Inferred from homology;
KW ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..200
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000181459"
SQ SEQUENCE 200 AA; 22711 MW; B2DC59A3919F983A CRC64;
MKIALFGTSA DPPTLAHRAI LIWLAQHFDQ VAVWAADNPF KQGPNPETGH WASLGDRQAM
LKLLVEDVQK DYATVQIWED LSDRRSLISL QRAQQRWGLE PDYALVVGAD LIRQISQWYA
VKELLPAVQL VIFPRPGYGI NQADLDKLAQ LGGHYQLVNQ GDDQAITPPI SSSIYRQIRD
DDLIPDPVQS YIQQRQLYRQ