(data stored in ACNUC1104 zone)

SWISSPROT: D3VHN1_XENNA

ID   D3VHN1_XENNA            Unreviewed;       346 AA.
AC   D3VHN1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00232078};
DE            EC=1.3.1.98 {ECO:0000256|HAMAP-Rule:MF_00037};
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00037};
GN   Name=murB {ECO:0000256|HAMAP-Rule:MF_00037,
GN   ECO:0000313|EMBL:CBJ88370.1};
GN   OrderedLocusNames=XNC1_0287 {ECO:0000313|EMBL:CBJ88370.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88370.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88370.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037,
CC       ECO:0000256|SAAS:SAAS00057166}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH +
CC         UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757;
CC         EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037,
CC         ECO:0000256|SAAS:SAAS01115694};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00037, ECO:0000256|SAAS:SAAS00170035};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00057202}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
CC       ECO:0000256|SAAS:SAAS00057122}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00037, ECO:0000256|SAAS:SAAS00558987}.
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DR   EMBL; FN667742; CBJ88370.1; -; Genomic_DNA.
DR   RefSeq; WP_010847798.1; NC_014228.1.
DR   STRING; 406817.XNC1_0287; -.
DR   EnsemblBacteria; CBJ88370; CBJ88370; XNC1_0287.
DR   KEGG; xne:XNC1_0287; -.
DR   eggNOG; ENOG4105D4A; Bacteria.
DR   eggNOG; COG0812; LUCA.
DR   HOGENOM; HOG000284356; -.
DR   KO; K00075; -.
DR   OMA; IGNAGSF; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.78.10; -; 1.
DR   HAMAP; MF_00037; MurB; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR003170; MurB.
DR   InterPro; IPR011601; MurB_C.
DR   InterPro; IPR036635; MurB_C_sf.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR21071; PTHR21071; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF02873; MurB_C; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   SUPFAM; SSF56194; SSF56194; 1.
DR   TIGRFAMs; TIGR00179; murB; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHN1.
DR   SWISS-2DPAGE; D3VHN1.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00445367};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00445259};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00445137};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00445388};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00098084};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098222};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00445343};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00445332};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00999659, ECO:0000313|EMBL:CBJ88370.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00445231};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN       17    187       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
FT   ACT_SITE    163    163       {ECO:0000256|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    233    233       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00037}.
FT   ACT_SITE    329    329       {ECO:0000256|HAMAP-Rule:MF_00037}.
SQ   SEQUENCE   346 AA;  38328 MW;  AB5D9BD32DB93407 CRC64;
     MFVYQSTQLK AFNTFSILAY ADHIVAATTI ESLLSLWQEA QRKNHPILLL GGGSNVLFTE
     NFKGTVILNR ILGINIQESD TAWHIHVGAG ENWHNLIISL LNQQIYGLEN LALIPGNVGS
     APIQNIGAYG IEFKHVCEYV DFIELESGNS IRLMTDECQF AYRDSIFKHQ YKDGYAITAV
     GLCLNKAWEP ILTYGSLTQL SRKDVTPEQI FHSVCEMRQS KLPDPAITGN AGSFFKNPII
     SPELAQKIKS QYPSCPQYHH NENSVKIAAG WLIDQCHLKG YSIGGAAVHT QQALVLVNKG
     NATGKDVIAL AAYVRSKVVE KFNIFLEPEV RFIGSQGEID AVECIS
//

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