(data stored in ACNUC7421 zone)

SWISSPROT: C5BCC1_EDWI9

ID   C5BCC1_EDWI9            Unreviewed;       345 AA.
AC   C5BCC1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00083566};
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   OrderedLocusNames=NT01EI_0160 {ECO:0000313|EMBL:ACR67412.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67412.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037,
CC       ECO:0000256|SAAS:SAAS00098160}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-
CC       N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH.
CC       {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098041}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00037, ECO:0000256|SAAS:SAAS00174316};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098068}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
CC       ECO:0000256|SAAS:SAAS00098013}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00037, ECO:0000256|SAAS:SAAS00551713}.
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DR   EMBL; CP001600; ACR67412.1; -; Genomic_DNA.
DR   RefSeq; WP_015869627.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0160; -.
DR   EnsemblBacteria; ACR67412; ACR67412; NT01EI_0160.
DR   GeneID; 7958975; -.
DR   KEGG; eic:NT01EI_0160; -.
DR   PATRIC; fig|634503.3.peg.147; -.
DR   eggNOG; ENOG4105D4A; Bacteria.
DR   eggNOG; COG0812; LUCA.
DR   HOGENOM; HOG000284356; -.
DR   KO; K00075; -.
DR   OMA; IGNAGSF; -.
DR   OrthoDB; POG091H02K7; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR003170; MurB.
DR   InterPro; IPR011601; MurB_C.
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; C5BCC1.
DR   SWISS-2DPAGE; C5BCC1.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057204};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057187};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057127};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057150};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057205};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00057134};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057194};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00057124};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057181, ECO:0000313|EMBL:ACR67412.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000256|SAAS:SAAS00057191};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       16    186       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
FT   ACT_SITE    162    162       {ECO:0000256|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    232    232       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00037}.
FT   ACT_SITE    328    328       {ECO:0000256|HAMAP-Rule:MF_00037}.
SQ   SEQUENCE   345 AA;  37821 MW;  3A6D50DAED35B6A5 CRC64;
     MSKHLTSLTE FTTFGLPARA EQILTADSAA VLLSHWQAAK ARRQPVLILG GGSNVLFMED
     FAGSVILNRI PGIQVDEDEV SWHLHVGAGE NWHDLVCYTL DHGMAGLENL ALIPGCVGSA
     PIQNIGAYGV ELQHVCDYVD ALDLRNGTLQ RLPATACGFG YRESIFKHRY RDGYAIVAVG
     LRLSKRWQPM LSYGDLTCLD AETATPRAVF DSVCHMRRTK LPDPAQHGNA GSFFKNPVVS
     AEAAEAIRAH YPQAPCYPQD NGEMKLAAGW LIDRCELKGY QIGGAAVHRQ QALVLINQHH
     ASAQNVIALA RYVRRRVGEV FSVWLEPEVR FIAAQGEVNA VEVLS
//

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