NNAAH_MYCPN
ID NNAAH_MYCPN Reviewed; 344 AA.
AC P75442;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=MPN_336; ORFNames=F10_orf291, MP500;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=10954595; DOI=10.1093/nar/28.17.3278;
RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U.,
RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., Yuan Y.P.,
RA Herrmann R., Bork P.;
RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding value,
RT function and reading frames.";
RL Nucleic Acids Res. 28:3278-3288(2000).
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 -!- 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; U00089; AAB96148.2; -; Genomic_DNA.
DR PIR; S73826; S73826.
DR AlphaFoldDB; P75442; -.
DR SMR; P75442; -.
DR STRING; 272634.MPN_336; -.
DR EnsemblBacteria; AAB96148; AAB96148; MPN_336.
DR KEGG; mpn:MPN_336; -.
DR HOGENOM; CLU_050191_0_0_14; -.
DR OMA; FHDICKE; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000000808; 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; 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..344
FT /note="Probable nicotinate-nucleotide
FT adenylyltransferase/Ap4A hydrolase"
FT /id="PRO_0000210478"
FT DOMAIN 193..304
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 1..182
FT /note="NaMN adenylyltransferase"
FT /evidence="ECO:0000305"
FT REGION 191..344
FT /note="Ap4A hydrolase"
FT /evidence="ECO:0000305"
FT BINDING 196
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 226..229
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 255
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 281..282
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 299
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 305
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
SQ SEQUENCE 344 AA; 39341 MW; 2910A628DECEDA19 CRC64;
MIFGGAFDPL HQAHIYIAKR AVQAIKAQKL YFVPTAKAFF KSPIKASNQA RLAMLRVALK
ALPQMAVSNF DIKAQNGFSF NTVQHFKQRF PNAELYFLIG SDKLSELAKW HNIEQLQKLC
RFVCYERFGY PIDEQLVQQF NVRLLGKCPL DLASSEMFGS HKFRQIPAKV LHYIHQHNIY
LKTILQTLLD EPRMQHCLRV GQLAKTLAVA NKLDGKTAYT AGAYHDLAKQ LPQAQLEKLA
KVAGVNDYPS WKVLHSYAGA YILKHWYGLN NSAVFSAIWN HTVPPQKMSQ LDMIIYLADK
LEPMRVHEEW AKGIDITALV KLAKKDLKLA YQITLKYVRS LQKN
