ID S5MJY5_9MOLU Unreviewed; 364 AA.
AC S5MJY5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:AGR42270.1};
GN ORFNames=SDIMI_v3c05660 {ECO:0000313|EMBL:AGR42270.1};
OS Spiroplasma diminutum CUAS-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276221 {ECO:0000313|EMBL:AGR42270.1, ECO:0000313|Proteomes:UP000014983};
RN [1] {ECO:0000313|EMBL:AGR42270.1, ECO:0000313|Proteomes:UP000014983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUAS-1 {ECO:0000313|EMBL:AGR42270.1};
RX PubMed=23873917; DOI=10.1093/gbe/evt108;
RA Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT "Comparison of metabolic capacities and inference of gene content evolution
RT in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL Genome Biol. Evol. 5:1512-1523(2013).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2
CC H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001682};
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}.
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DR EMBL; CP005076; AGR42270.1; -; Genomic_DNA.
DR RefSeq; WP_020836502.1; NC_021833.1.
DR AlphaFoldDB; S5MJY5; -.
DR STRING; 1276221.SDIMI_v3c05660; -.
DR KEGG; sdi:SDIMI_v3c05660; -.
DR PATRIC; fig|1276221.3.peg.565; -.
DR eggNOG; COG1057; Bacteria.
DR eggNOG; COG1713; Bacteria.
DR HOGENOM; CLU_050191_0_0_14; -.
DR InParanoid; S5MJY5; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000014983; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:RHEA.
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; cd00077; HDc; 1.
DR CDD; cd02165; NMNAT; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR HAMAP; MF_00244; NaMN_adenylyltr; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR005249; YqeK.
DR NCBIfam; TIGR00488; bis(5'-nucleosyl)-tetraphosphatase (symmetrical) YqeK; 1.
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 Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
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:AGR42270.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000014983};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:AGR42270.1}.
FT DOMAIN 193..318
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
SQ SEQUENCE 364 AA; 42647 MW; E1296E8B88948D6D CRC64;
MKKIALFGGS FDPVHTDHIN IIKSCKTNLN FDEVWVIPAY VNPFKTLSTS SVTQRLEMLK
LATMDLNFVK IETYEISKQT SSFTHDTVKY YKSKYPDLEF SFIMGSDQLD NFEKWDHFSE
LIQEIDFKVF LRSKEFNQEI VEKYNLETFE FENNYLSSTK IRNLEDLNLQ IKSVNDYVNN
NLMYLYERLE SRMDEKRYFH CLNVGQMAME LARLNNIDLN KAQIAGTLHD IAKRWTEEEL
KECLLKNDPS LLKEPVPVWH SYAGAFHLKN DWLMNDAEII NSVYNHTVGS KDMTTLDIIV
FCADKISLER TYPGVEKLRA LVKSDLLLGF KELLKNQYEV AINKNTKNSI GMKLIESYDY
WIKG
//
