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NADD_MYCTU
ID   NADD_MYCTU              Reviewed;         214 AA.
AC   P9WJJ5; L0TCA5; O86328;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE            EC=2.7.7.18 {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE            Short=NaMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
GN   Name=nadD {ECO:0000255|HAMAP-Rule:MF_00244}; OrderedLocusNames=Rv2421c;
GN   ORFNames=MTCY428.26;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-42, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000255|HAMAP-Rule:MF_00244}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00244};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00244}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00244, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP45212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP45212.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70685; H70685.
DR   RefSeq; NP_216937.1; NC_000962.3.
DR   RefSeq; WP_003412398.1; NZ_NVQJ01000054.1.
DR   PDB; 4RPI; X-ray; 2.42 A; A/B/C/D=4-214.
DR   PDB; 4S1O; X-ray; 1.84 A; A/B=4-195.
DR   PDB; 4X0E; X-ray; 2.41 A; A/B=4-214.
DR   PDB; 4YBR; X-ray; 1.65 A; A/B=4-195.
DR   PDB; 5DAS; X-ray; 2.20 A; A/B/C/D=4-195.
DR   PDB; 6BUV; X-ray; 1.86 A; A/B=4-195.
DR   PDBsum; 4RPI; -.
DR   PDBsum; 4S1O; -.
DR   PDBsum; 4X0E; -.
DR   PDBsum; 4YBR; -.
DR   PDBsum; 5DAS; -.
DR   PDBsum; 6BUV; -.
DR   AlphaFoldDB; P9WJJ5; -.
DR   SMR; P9WJJ5; -.
DR   STRING; 83332.Rv2421c; -.
DR   PaxDb; P9WJJ5; -.
DR   DNASU; 885457; -.
DR   GeneID; 885457; -.
DR   KEGG; mtu:Rv2421c; -.
DR   TubercuList; Rv2421c; -.
DR   eggNOG; COG1057; Bacteria.
DR   OMA; IHIGHLI; -.
DR   PhylomeDB; P9WJJ5; -.
DR   BRENDA; 2.7.7.18; 3445.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000001584; 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; Direct protein sequencing; NAD;
KW   Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181427"
FT   STRAND          1..3
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           10..22
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:6BUV"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           68..72
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:4S1O"
FT   HELIX           78..88
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           100..109
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           112..118
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           129..132
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           134..144
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           160..168
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   HELIX           179..187
FT                   /evidence="ECO:0007829|PDB:4YBR"
FT   TURN            188..191
FT                   /evidence="ECO:0007829|PDB:4YBR"
SQ   SEQUENCE   214 AA;  23340 MW;  D4F2D71B86F30385 CRC64;
     MGVMGGTFDP IHYGHLVAAS EVADLFDLDE VVFVPSGQPW QKGRQVSAAE HRYLMTVIAT
     ASNPRFSVSR VDIDRGGPTY TKDTLADLHA LHPDSELYFT TGADALASIM SWQGWEELFE
     LARFVGVSRP GYELRNEHIT SLLGQLAKDA LTLVEIPALA ISSTDCRQRA EQSRPLWYLM
     PDGVVQYVSK CRLYCGACDA GARSTTSLAA GNGL
 
 
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