(data stored in ACNUC7421 zone)

SWISSPROT: Q13IK1_PARXL

ID   Q13IK1_PARXL            Unreviewed;       284 AA.
AC   Q13IK1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00694129};
DE            EC=6.3.1.5 {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00694131};
GN   Name=nadE {ECO:0000256|HAMAP-Rule:MF_00193};
GN   ORFNames=Bxe_C0163 {ECO:0000313|EMBL:ABE36088.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36088.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36088.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36088.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to
CC       form NAD. Uses ammonia as a nitrogen source. {ECO:0000256|HAMAP-
CC       Rule:MF_00193, ECO:0000256|SAAS:SAAS00821813}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+)
CC         + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215;
CC         EC=6.3.1.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00193,
CC         ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS01118362};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00193, ECO:0000256|RuleBase:RU004252,
CC       ECO:0000256|SAAS:SAAS00694141}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00193,
CC       ECO:0000256|SAAS:SAAS00821812}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811,
CC       ECO:0000256|SAAS:SAAS00694133}.
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DR   EMBL; CP000272; ABE36088.1; -; Genomic_DNA.
DR   RefSeq; WP_011493348.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0163; -.
DR   EnsemblBacteria; ABE36088; ABE36088; Bxe_C0163.
DR   GeneID; 4009711; -.
DR   KEGG; bxb:DR64_8266; -.
DR   KEGG; bxe:Bxe_C0163; -.
DR   PATRIC; fig|266265.5.peg.7944; -.
DR   eggNOG; ENOG4107RW9; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   HOGENOM; HOG000238070; -.
DR   KO; K01916; -.
DR   OMA; NAGERFR; -.
DR   OrthoDB; 1152435at2; -.
DR   BioCyc; BXEN266265:BXE_RS37550-MONOMER; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0008795; F:NAD+ synthase 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   HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR003694; NAD_synthase.
DR   InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR23090; PTHR23090; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   TIGRFAMs; TIGR00552; nadE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13IK1.
DR   SWISS-2DPAGE; Q13IK1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702598};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702604,
KW   ECO:0000313|EMBL:ABE36088.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|SAAS:SAAS00821815};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|SAAS:SAAS00821809};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702606};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702608};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       34    276       NAD_synthase. {ECO:0000259|Pfam:PF02540}.
FT   NP_BIND      54     61       ATP. {ECO:0000256|HAMAP-Rule:MF_00193}.
FT   NP_BIND     271    272       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
FT   METAL        60     60       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
FT   METAL       176    176       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
FT   BINDING     151    151       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
FT   BINDING     171    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00193}.
FT   BINDING     184    184       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
FT   BINDING     191    191       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
FT   BINDING     200    200       ATP. {ECO:0000256|HAMAP-Rule:MF_00193}.
FT   BINDING     222    222       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00193}.
SQ   SEQUENCE   284 AA;  31136 MW;  C2718575909F8B80 CRC64;
     MNPSSSPYGN AWQQEVLSEL GVPRDFDVDA ERERRIGFLG DYLASQGLRT YVLGISGGVD
     SSTAGRLAQL AVDRLRARGY EAKFLAVRLP YGSQRDEEDA ALALEFIRPD ETLTVNIKEP
     SDAMLQSLKR GGAQYVDDFQ EDFVLGNIKA RQRMVAQYAI AGARVGVVIG TDHAAESLMG
     FFTKYGDGGA DILPLSGLTK RRVRALARAL GASERLANKV PTADLESLTP QKPDEDSYGI
     SYEDIDDFLE GKPVSDEVLT TIRRFHTATR HKRALPVSVN PANR
//

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