(data stored in SCRATCH zone)

SWISSPROT: D4YXS3_SPHJU

ID   D4YXS3_SPHJU            Unreviewed;       553 AA.
AC   D4YXS3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   05-JUL-2017, entry version 45.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|PIRNR:PIRNR006630};
DE            EC=6.3.5.1 {ECO:0000256|PIRNR:PIRNR006630};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|PIRNR:PIRNR006630};
GN   Name=nadE {ECO:0000313|EMBL:BAI95155.1};
GN   OrderedLocusNames=SJA_C1-03210 {ECO:0000313|EMBL:BAI95155.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95155.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95155.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC       AMP + diphosphate + NAD(+) + L-glutamate.
CC       {ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family.
CC       {ECO:0000256|RuleBase:RU003811}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD
CC       synthetase family. {ECO:0000256|PIRNR:PIRNR006630}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010803; BAI95155.1; -; Genomic_DNA.
DR   RefSeq; WP_013038942.1; NC_014006.1.
DR   ProteinModelPortal; D4YXS3; -.
DR   STRING; 452662.SJA_C1-03210; -.
DR   EnsemblBacteria; BAI95155; BAI95155; SJA_C1-03210.
DR   GeneID; 29272023; -.
DR   KEGG; sjp:SJA_C1-03210; -.
DR   eggNOG; ENOG4105C4K; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   eggNOG; COG0388; LUCA.
DR   HOGENOM; HOG000226694; -.
DR   KO; K01916; -.
DR   OMA; CEDIWND; -.
DR   OrthoDB; POG091H00G3; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00553; NAD_synthase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR014445; Gln-dep_NAD_synthase.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR003694; NAD_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR23090; PTHR23090; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PIRSF; PIRSF006630; NADS_GAT; 2.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   TIGRFAMs; TIGR00552; nadE; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXS3.
DR   SWISS-2DPAGE; D4YXS3.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR006630,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702598};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Ligase {ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702604, ECO:0000313|EMBL:BAI95155.1};
KW   NAD {ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702606};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006630,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702608};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        5    269       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
SQ   SEQUENCE   553 AA;  61182 MW;  1C57FA18F33E4822 CRC64;
     MTDKLVIALA QMTQSVGDLA ANADAMLEWR TRAMEADLIV YPELQLIGYP PEDLVLKPAL
     VDRANHELDR LAQATADGGP AMLVGTVVAS QGVLFNVVAL LEDGAVTAIR QKRELPNYGT
     FDEKRLFAPG PLPAPIDFRG VKIGVPICED IWFPFVTAHL RAEGAEILIS PNGSPFEVDK
     DDRRINAVAG TRVRETGLPL VYLNRVGGQD ELVFDGASFV MNGDLSLAHQ LPDWEEALVL
     THWEKWEGQW VCLPGERHVL DERPADIYNA MVLGLRDYVN KNRFPGVVLG LSGGIDSALS
     AAVAVDALGA DRVWCVMMPS RFTSRESLDD AIECARLLGV RYDSIPIEPA VEAFDAMLAD
     VFTGRQRDLT EENIQSRIRG VTLMALSNKY GHMLLTTGNK SEMSVGYATI YGDMAGGYSV
     LKDAYKTTVF DLCRWRNENV PSLGEAFGPE GPVMPDRVIT KPPSAELRDN QKDEDSLPPY
     EVLDPILYGL VEEELSVEQL VARGFDKDTV ARIERLLYVA EYKRRQSPPG VKLGMRNFGR
     DRRYPITNAF RTL
//

If you have problems or comments...

PBIL Back to PBIL home page