NNAAH_UREPA
ID NNAAH_UREPA Reviewed; 392 AA.
AC Q9PQ21;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
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 Name=nadD; OrderedLocusNames=UU469;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(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; AF222894; AAF30881.1; -; Genomic_DNA.
DR RefSeq; WP_006688791.1; NC_002162.1.
DR AlphaFoldDB; Q9PQ21; -.
DR SMR; Q9PQ21; -.
DR STRING; 273119.UU469; -.
DR PRIDE; Q9PQ21; -.
DR EnsemblBacteria; AAF30881; AAF30881; UU469.
DR GeneID; 29672541; -.
DR KEGG; uur:UU469; -.
DR eggNOG; COG1057; Bacteria.
DR eggNOG; COG1713; Bacteria.
DR HOGENOM; CLU_050191_0_0_14; -.
DR OMA; FHDICKE; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000000423; 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: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..392
FT /note="Probable nicotinate-nucleotide
FT adenylyltransferase/Ap4A hydrolase"
FT /id="PRO_0000181465"
FT DOMAIN 232..355
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 1..210
FT /note="NaMN adenylyltransferase"
FT /evidence="ECO:0000305"
FT REGION 230..392
FT /note="Ap4A hydrolase"
FT /evidence="ECO:0000305"
FT BINDING 235
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 266..269
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 300
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 326..327
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 350
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 356
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
SQ SEQUENCE 392 AA; 46645 MW; 4897A34B2876725C CRC64;
MKIILFCGAF DMVHNAHIAM AKQAMKLVNA DKLIFLPSNF KFFKAINKND NLEYEKTKLT
PGHHRIAMLK IATKNLVNIE VSDYELKQIN KSYTINTIEH FKQIYGSEHE YYFIMGSDNL
ERFKQWKDWE RILKEVKIIC FKRGDVCVKK SCPQKSCECE SFNFFEHEIL LVNDFNYNIS
STEIKKRHNL TSGIDPAVLD YINEHGLYAL WLLEKHLISY DNFNNLEKKV ARINHCRRVA
QMCVDLMNVY DKKLIDQAYC AGIYHDILKC LDEQESVAYF NEHKSELNIG DDFISWRILH
SYLGAHLLQT QYGFKNQLIL NAIRRHTRPF DFIKDYSELT TLDKILYCAD KLEPNRREEI
DQINIDYYRK LVFEDLDKAF IEVYQYQQRQ RK
