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NADD_PSEAE
ID   NADD_PSEAE              Reviewed;         214 AA.
AC   Q9HX21;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase;
DE            EC=2.7.7.18;
DE   AltName: Full=Deamido-NAD(+) diphosphorylase;
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase;
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase;
DE            Short=NaMN adenylyltransferase;
GN   Name=nadD; OrderedLocusNames=PA4006;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000250}.
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG07393.1; -; Genomic_DNA.
DR   PIR; B83147; B83147.
DR   RefSeq; NP_252695.1; NC_002516.2.
DR   RefSeq; WP_003093199.1; NZ_QZGE01000038.1.
DR   PDB; 1YUL; X-ray; 2.00 A; A=1-214.
DR   PDB; 1YUM; X-ray; 1.70 A; A/B/C/D=1-214.
DR   PDB; 1YUN; X-ray; 2.00 A; A/B=1-214.
DR   PDBsum; 1YUL; -.
DR   PDBsum; 1YUM; -.
DR   PDBsum; 1YUN; -.
DR   AlphaFoldDB; Q9HX21; -.
DR   SMR; Q9HX21; -.
DR   STRING; 287.DR97_3861; -.
DR   PaxDb; Q9HX21; -.
DR   PRIDE; Q9HX21; -.
DR   EnsemblBacteria; AAG07393; AAG07393; PA4006.
DR   GeneID; 878969; -.
DR   KEGG; pae:PA4006; -.
DR   PATRIC; fig|208964.12.peg.4198; -.
DR   PseudoCAP; PA4006; -.
DR   HOGENOM; CLU_069765_0_0_6; -.
DR   InParanoid; Q9HX21; -.
DR   OMA; IHIGHLI; -.
DR   PhylomeDB; Q9HX21; -.
DR   BioCyc; PAER208964:G1FZ6-4079-MON; -.
DR   BRENDA; 2.7.7.18; 5087.
DR   UniPathway; UPA00253; UER00332.
DR   EvolutionaryTrace; Q9HX21; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00482; TIGR00482; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181432"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           17..30
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           53..64
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           85..95
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           112..116
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           146..152
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           179..187
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   HELIX           198..206
FT                   /evidence="ECO:0007829|PDB:1YUM"
FT   TURN            207..210
FT                   /evidence="ECO:0007829|PDB:1YUM"
SQ   SEQUENCE   214 AA;  23801 MW;  95FF8237AD0C3A69 CRC64;
     MGKRIGLFGG TFDPVHIGHM RSAVEMAEQF ALDELRLLPN ARPPHRETPQ VSAAQRLAMV
     ERAVAGVERL TVDPRELQRD KPSYTIDTLE SVRAELAADD QLFMLIGWDA FCGLPTWHRW
     EALLDHCHIV VLQRPDADSE PPESLRDLLA ARSVADPQAL KGPGGQITFV WQTPLAVSAT
     QIRALLGAGR SVRFLVPDAV LNYIEAHHLY RAPH
 
 
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