ID   NNAAH_MYCGE             Reviewed;         350 AA.
AC   P47482;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase/Ap4A hydrolase {ECO:0000305};
DE   Includes:
DE     RecName: Full=Nicotinate-nucleotide adenylyltransferase {ECO:0000250|UniProtKB:P0A752};
DE              EC=2.7.7.18 {ECO:0000250|UniProtKB:P0A752};
DE     AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000250|UniProtKB:P0A752};
DE     AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000250|UniProtKB:P0A752};
DE     AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000250|UniProtKB:P0A752};
DE              Short=NaMN adenylyltransferase {ECO:0000250|UniProtKB:P0A752};
DE   Includes:
DE     RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000250|UniProtKB:Q2G297};
DE              EC=3.6.1.41 {ECO:0000250|UniProtKB:Q2G297};
DE     AltName: Full=Ap4A hydrolase {ECO:0000250|UniProtKB:Q2G297};
GN   OrderedLocusNames=MG240;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-350.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
RN   [3]
RP   SEQUENCE REVISION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA   Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA   Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT   "Essential genes of a minimal bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000250|UniProtKB:P0A752}.
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to
CC       yield ADP. {ECO:0000250|UniProtKB:Q2G297}.
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:0000250|UniProtKB:P0A752};
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:0000250|UniProtKB:Q2G297};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000250|UniProtKB:P0A752}.
CC   -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC       global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NadD family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Ap4A hydrolase
CC       YqeK family. {ECO:0000305}.
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DR   EMBL; L43967; AAC71461.2; -; Genomic_DNA.
DR   EMBL; U01734; AAD10544.1; -; Genomic_DNA.
DR   PIR; E64226; E64226.
DR   RefSeq; WP_010869387.1; NC_000908.2.
DR   AlphaFoldDB; P47482; -.
DR   SMR; P47482; -.
DR   STRING; 243273.MG_240; -.
DR   KEGG; mge:MG_240; -.
DR   eggNOG; COG1057; Bacteria.
DR   eggNOG; COG1713; Bacteria.
DR   HOGENOM; CLU_050191_0_0_14; -.
DR   InParanoid; P47482; -.
DR   OrthoDB; 5295945at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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; 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; PTHR35795:SF1; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE, SYMMETRICAL; 1.
DR   PANTHER; PTHR35795; SLR1885 PROTEIN; 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.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Iron; Metal-binding; Multifunctional enzyme; NAD;
KW   Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..350
FT                   /note="Probable nicotinate-nucleotide
FT                   adenylyltransferase/Ap4A hydrolase"
FT                   /id="PRO_0000210477"
FT   DOMAIN          198..310
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..187
FT                   /note="NaMN adenylyltransferase"
FT                   /evidence="ECO:0000305"
FT   REGION          196..350
FT                   /note="Ap4A hydrolase"
FT                   /evidence="ECO:0000305"
FT   BINDING         201
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         230
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         231..234
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         231
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         261
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         287..288
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         305
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         305
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT   BINDING         311
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KD90"
SQ   SEQUENCE   350 AA;  40217 MW;  772554F49052B335 CRC64;
     MKQKIIIFGG SFDPIHNAHL YIAKHAIKKI KAQKLFFVPT YNGIFKNNFH ASNKDRIAML
     KLAIKSVNNA LVSNFDIKTK NAFSINTVNH FKSCYPTSEI YFLIGSDKLN ELEKWDHIQQ
     LKDLCTFVCY ERKPYPFNKK IANQFNVKYL AKCPLEIASS KLLNQPRKKL IPLAVLNYIN
     TNHLYLIPTL KAMVDDKRFQ HCLRVGKLAK QLAIANKLDA KRAFVAGAYH DLAKQLPVDQ
     LVNIATSELK ITNYPSWKVL HSYVGAYILK NWFGVKDKMI INAIKNHTIP PKQVSKLDMI
     VYLADKLEPN RKQEQWSGGI EIDQLVKLAK SNLKQAYLIT LKYVQNLVKD
//