NADD_RHOBA
ID NADD_RHOBA Reviewed; 214 AA.
AC Q7UFN6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE EC=2.7.7.18 {ECO:0000255|HAMAP-Rule:MF_00244};
DE AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE Short=NaMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
GN Name=nadD {ECO:0000255|HAMAP-Rule:MF_00244}; OrderedLocusNames=RB8455;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00244};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00244}.
CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000255|HAMAP-
CC Rule:MF_00244}.
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DR EMBL; BX294147; CAD78646.1; -; Genomic_DNA.
DR RefSeq; NP_868368.1; NC_005027.1.
DR AlphaFoldDB; Q7UFN6; -.
DR SMR; Q7UFN6; -.
DR STRING; 243090.RB8455; -.
DR EnsemblBacteria; CAD78646; CAD78646; RB8455.
DR KEGG; rba:RB8455; -.
DR PATRIC; fig|243090.15.peg.4065; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_0_1_0; -.
DR InParanoid; Q7UFN6; -.
DR OMA; IHIGHLI; -.
DR OrthoDB; 1433958at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000001025; 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; TIGR00125; cyt_tran_rel; 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..214
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000181435"
SQ SEQUENCE 214 AA; 24192 MW; A96D2375096161CF CRC64;
MSASETTPQS NHGIGILGGS FDPVHVGHLW MAESALEQLP IEHVRWIPAA TSPLKPHGPV
ASNEHRLQML RLALSGQSGL VIDDWELRQD SVSYTLLTLE YLQEQFPDRP LYLIIGADSL
ASFDRWREPE QILKRCHLAV IARGGDPPPD YSILDGMTDE TQIQRIRESQ IQMPQIEISS
SDLRNRIATG RSIRFRVPHP VATLIDNEKM YRVR