NNAAH_MYCGE
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 03-AUG-2022, entry version 111.
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; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
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 EnsemblBacteria; AAC71461; AAC71461; MG_240.
DR KEGG; mge:MG_240; -.
DR eggNOG; COG1057; Bacteria.
DR eggNOG; COG1713; Bacteria.
DR HOGENOM; CLU_050191_0_0_14; -.
DR OrthoDB; 1433958at2; -.
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; -; 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 Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
DR TIGRFAMs; TIGR00488; TIGR00488; 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
