(data stored in ACNUC1104 zone)

SWISSPROT: D7A0V8_STAND

ID   D7A0V8_STAND            Unreviewed;       429 AA.
AC   D7A0V8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN   OrderedLocusNames=Snov_0131 {ECO:0000313|EMBL:ADH87468.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87468.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87468.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-
CC         glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483;
CC         EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111,
CC         ECO:0000256|SAAS:SAAS01124343};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767211}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002026; ADH87468.1; -; Genomic_DNA.
DR   RefSeq; WP_013164973.1; NC_014217.1.
DR   STRING; 639283.Snov_0131; -.
DR   EnsemblBacteria; ADH87468; ADH87468; Snov_0131.
DR   KEGG; sno:Snov_0131; -.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; 537477at2; -.
DR   BioCyc; SNOV639283:G1GLM-132-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase 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   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00111; MurA; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A0V8.
DR   SWISS-2DPAGE; D7A0V8.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767221};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767191};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767246};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767261};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767234};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767219};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:ADH87468.1}.
FT   DOMAIN        8    417       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   REGION      171    174       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    126    126       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   BINDING     102    102       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     316    316       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     338    338       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   MOD_RES     126    126       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   429 AA;  45450 MW;  F928CDAB7F4FCE14 CRC64;
     MDRIRIVGGN PLTGSIPISG AKNAALPLMI AGLLTDEKLV LHNVPRLADV SQLQRILGNH
     GIDITVNGKR RGDDPYSGQT MEIDARVIVD TTAPYELVSK MRASFWVIGP LVARMGEAKV
     SLPGGCAIGT RPVDFHLDAL RALGAEIEID AGYVLARAPK GLKGAHILFP KVSVGATHTA
     MMAASLAEGE TILENAAREP EIVDVADCIN AMGGRIEGQG TSTIRITGVP RLKGAHHSVL
     PDRIETGTYA MAVAMTGGDV MLSGARADLL DSALDTLREC GAEVTVSNEG LRVKRNGAGI
     SPVEVTTAPF PGFPTDLQAQ LMALTTRARG TSKITETIFE NRFMHVQELA RLGARIHLDG
     EIATIEGVEK LKGAPVMATD LRASVSLVIG ALAAEGESMI HRVYHLDRGF ERLEEKLSAC
     GAEIERLAG
//

If you have problems or comments...

PBIL Back to PBIL home page