(data stored in ACNUC7421 zone)

HOGENOM: STRE4_1_PE1003

ID   STRE4_1_PE1003                       STANDARD;      PRT;   295 AA.
AC   STRE4_1_PE1003; C0MA63;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase; EC=1.1.1
DE   158;AltName: Full=UDP-N-acetylmuramate dehydrogenase; (STRE4_1.PE1003).
GN   Name=murB; OrderedLocusNames=SEQ_1128;
OS   STREPTOCOCCUS EQUI SUBSP. EQUI 4047.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=553482;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STRE4_1.PE1003.
CC       Streptococcus equi subsp. equi 4047, complete genome.
CC       chromosome 1, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MURB_STRE4
CC   -!- FUNCTION: Cell wall formation (By similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl-
CC       3-O-(1-carboxyvinyl)-D-glucosamine + NADPH.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murB family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
CC   -!- GENE_FAMILY: HOG000284355 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C0MA63; -.
DR   EMBL; FM204883; CAW93799.1; -; Genomic_DNA.
DR   RefSeq; YP_002746437.1; NC_012471.1.
DR   STRING; C0MA63; -.
DR   EnsemblBacteria; EBSTRT00000068173; EBSTRP00000062373; EBSTRG00000068184.
DR   GeneID; 7696074; -.
DR   GenomeReviews; FM204883_GR; SEQ_1128.
DR   KEGG; seu:SEQ_1128; -.
DR   GeneTree; EBGT00050000027116; -.
DR   OMA; SKKHAGF; -.
DR   ProtClustDB; PRK13905; -.
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:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
DR   Gene3D; G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
DR   Gene3D; G3DSA:3.90.78.10; MurB_C; 1.
DR   PANTHER; PTHR21071; MurB; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF02873; MurB_C; 1.
DR   SUPFAM; SSF56176; FAD-binding_2; 1.
DR   SUPFAM; SSF56194; MurB_C; 1.
DR   TIGRFAMs; TIGR00179; MurB; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   HOGENOMDNA; STRE4_1.PE1003; -.
KW   Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD;
KW   Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis.
SQ   SEQUENCE   295 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIAELEGIDI RENEALKHYT YTQVGGPADF LAFPRNHYEL SRIVDYANHN HIPWMVLGNA
     SNLIVRDGGI RGFVIMFDKL NAVRLNGYTL EAEAGANLIE TTKVAKFHSL TGFEFACGIP
     GSIGGAVFMN AGAYGGEIAH IFLSAKVLTP EGKIKKISAR EMAFGYRHSV IQETGDIVIS
     AKFALKPGNH DSICQEMNRL NHLRKLKQPL EFPSCGSVFK RPPGHFAGQL IMDANLKGHR
     VGGVEVSKKH AGFMINVADG SAKDYEDLIA HVIRTVEQAS GVRLEPEVRI IGESL
//

If you have problems or comments...

PBIL Back to PBIL home page