MURB_STRCO
ID MURB_STRCO Reviewed; 383 AA.
AC Q9L0L7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000255|HAMAP-Rule:MF_00037};
DE EC=1.3.1.98 {ECO:0000255|HAMAP-Rule:MF_00037};
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00037};
GN Name=murB {ECO:0000255|HAMAP-Rule:MF_00037}; OrderedLocusNames=SCO4643;
GN ORFNames=SCD82.14;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-
CC 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; EC=1.3.1.98;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00037};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00037}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000255|HAMAP-
CC Rule:MF_00037}.
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DR EMBL; AL939120; CAB77417.1; -; Genomic_DNA.
DR RefSeq; NP_628804.1; NC_003888.3.
DR RefSeq; WP_011029789.1; NC_003888.3.
DR AlphaFoldDB; Q9L0L7; -.
DR SMR; Q9L0L7; -.
DR STRING; 100226.SCO4643; -.
DR GeneID; 1100084; -.
DR KEGG; sco:SCO4643; -.
DR PATRIC; fig|100226.15.peg.4714; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_0_1_11; -.
DR InParanoid; Q9L0L7; -.
DR OMA; MQNIGAY; -.
DR PhylomeDB; Q9L0L7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..383
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179268"
FT DOMAIN 49..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 271
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 375
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ SEQUENCE 383 AA; 40364 MW; 51BA5E7DB3B19466 CRC64;
MRTRRDVPAD RSGRSRVSRH PGLSVPSRTL EPVQELHDAP LAPLTTFRLG GPATRLLTAT
TDAEVIAAVR EADDTGTPLL LIGGGSNLVI GDKGFDGTAL HIATRGFRLD GTTLELAAGE
IWTDAVARTV EAGLAGVECL AGIPGSAGAT PIQNVGAYGQ EVSATITEVT AYDRRSGETV
ALSNADCAFS YRHSRFKAEP ERYVVLRVRF ELENADGLSA PLRYAETARA LGVEAGDRVP
LTAARETVLR LRAGKGMVLD PEDHDTWSAG SFFTNPILTD EEFAAFRSRV AGRLGAAVEP
PAFPAGEGRV KTSAAWLIDK AGFTKGYGTG PARISTKHTL ALTNRGEATT EDLLALAREV
VAGVHEAFGV TLVNEPVTVG VAL
