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Database: UniProt
Entry: F6EUD8_SPHCR
LinkDB: F6EUD8_SPHCR
Original site: F6EUD8_SPHCR 
ID   F6EUD8_SPHCR            Unreviewed;       209 AA.
AC   F6EUD8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE            EC=2.7.7.18 {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE            Short=NaMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
GN   Name=nadD {ECO:0000256|HAMAP-Rule:MF_00244};
GN   ORFNames=Sphch_1914 {ECO:0000313|EMBL:AEG49591.1};
OS   Sphingobium chlorophenolicum L-1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG49591.1, ECO:0000313|Proteomes:UP000007150};
RN   [1] {ECO:0000313|EMBL:AEG49591.1, ECO:0000313|Proteomes:UP000007150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-1 {ECO:0000313|EMBL:AEG49591.1,
RC   ECO:0000313|Proteomes:UP000007150};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT   "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-
RT   1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide
CC       (NaAD). {ECO:0000256|HAMAP-Rule:MF_00244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-
CC         NAD(+) + 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:0000256|HAMAP-
CC         Rule:MF_00244};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
CC       NAD(+) from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00244}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00244, ECO:0000256|SAAS:SAAS01025576}.
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DR   EMBL; CP002798; AEG49591.1; -; Genomic_DNA.
DR   RefSeq; WP_013847839.1; NC_015593.1.
DR   EnsemblBacteria; AEG49591; AEG49591; Sphch_1914.
DR   GeneID; 35852495; -.
DR   KEGG; sch:Sphch_1914; -.
DR   eggNOG; ENOG4107WK2; Bacteria.
DR   eggNOG; COG1057; LUCA.
DR   KO; K00969; -.
DR   OrthoDB; 1433958at2; -.
DR   BioCyc; SCHL690566:G1GN4-1929-MONOMER; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000007150; Chromosome 1.
DR   GO; GO:0005524; F:ATP 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459924};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007150};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000256|SAAS:SAAS00459916};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459927};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459933, ECO:0000313|EMBL:AEG49591.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007150};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:AEG49591.1}.
FT   DOMAIN        6    184       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   209 AA;  24108 MW;  6ECF0D625F1B6C05 CRC64;
     MKRIGLLGGS FNPAHGGHRA ISLFAAKTLR LDEIWWLVSP GNPLKPKTGM APLPARLAHA
     RKVARRTPIR PTAIEAQLGT RYTIDSLKAL RRRYPRHRFL WLMGADNLAQ FGQWRDWRGI
     ARTMPIAVIA RPGYDKAARG SPAMSWLRRF VRPARQSADW TDWRLPALVL LRFRPDPRSA
     TLLRQADPLW HREYSETRVR DPLTRRMIV
//
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