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Multifunctional fusion protein [Includes: UDP-N-acetylenolpyruvoylglucosamine reductase (EC 1.3.1.98) (UDP-N-acetylmuramate dehydrogenase); UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); UDP-N-acetylmuramyl-tripeptide synthetase (EC 6.3.2.-) (UDP-MurNAc-tripeptide synthetase)]

 A0A0G1C4S4_9BACT        Unreviewed;      1220 AA.
A0A0G1C4S4;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
16-JAN-2019, entry version 38.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|HAMAP-Rule:MF_00208};
Includes:
RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|HAMAP-Rule:MF_00037};
EC=1.3.1.98 {ECO:0000256|HAMAP-Rule:MF_00037};
AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00037};
Includes:
RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00046};
EC=6.3.2.8 {ECO:0000256|HAMAP-Rule:MF_00046};
AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
Includes:
RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
EC=6.3.2.- {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
Synonyms=murB {ECO:0000256|HAMAP-Rule:MF_00037},
murC {ECO:0000256|HAMAP-Rule:MF_00046};
ORFNames=UV56_C0017G0004 {ECO:0000313|EMBL:KKS80449.1};
Candidatus Woesebacteria bacterium GW2011_GWC1_43_10b.
Bacteria; Candidatus Woesebacteria.
NCBI_TaxID=1618585 {ECO:0000313|EMBL:KKS80449.1};
[1] {ECO:0000313|EMBL:KKS80449.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
Wilkins M.J., Williams K.H., Banfield J.F.;
"rRNA introns, odd ribosomes, and small enigmatic genomes across a
large radiation of phyla.";
Nature 0:0-0(2015).
-!- FUNCTION: Catalyzes the addition of an amino acid to the
nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
(UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS01090476}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP +
H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
Evidence={ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS01124320};
-!- CATALYTIC ACTIVITY:
Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH +
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757;
EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS01115694};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00174316};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00382155}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00382163}.
-!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
consequently, for the gamma-phosphate positioning of ATP.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
Rule:MF_00037, ECO:0000256|SAAS:SAAS00558987}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KKS80449.1}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; LCEY01000017; KKS80449.1; -; Genomic_DNA.
EnsemblBacteria; KKS80449; KKS80449; UV56_C0017G0004.
PATRIC; fig|1618585.3.peg.224; -.
UniPathway; UPA00219; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
Gene3D; 3.40.1190.10; -; 2.
Gene3D; 3.90.190.20; -; 2.
Gene3D; 3.90.78.10; -; 1.
HAMAP; MF_00037; MurB; 1.
HAMAP; MF_00046; MurC; 1.
HAMAP; MF_00208; MurE; 1.
InterPro; IPR016166; FAD-bd_PCMH.
InterPro; IPR036318; FAD-bd_PCMH-like_sf.
InterPro; IPR016167; FAD-bd_PCMH_sub1.
InterPro; IPR016169; FAD-bd_PCMH_sub2.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR003170; MurB.
InterPro; IPR011601; MurB_C.
InterPro; IPR036635; MurB_C_sf.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC.
Pfam; PF01565; FAD_binding_4; 1.
Pfam; PF01225; Mur_ligase; 2.
Pfam; PF02875; Mur_ligase_C; 2.
Pfam; PF08245; Mur_ligase_M; 2.
Pfam; PF02873; MurB_C; 1.
SUPFAM; SSF53244; SSF53244; 2.
SUPFAM; SSF53623; SSF53623; 2.
SUPFAM; SSF56176; SSF56176; 1.
SUPFAM; SSF56194; SSF56194; 1.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR00179; murB; 1.
TIGRFAMs; TIGR01082; murC; 1.
PROSITE; PS51387; FAD_PCMH; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00084995};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00085032};
Cell division {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00085032};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00085152};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00085135};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00085104};
FAD {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00990849};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00990849};
Ligase {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00085127, ECO:0000313|EMBL:KKS80449.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
NADP {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00057124};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00084995};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00991263};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00085152}.
DOMAIN 927 1090 FAD-binding PCMH-type.
{ECO:0000259|PROSITE:PS51387}.
NP_BIND 98 104 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
NP_BIND 547 553 ATP. {ECO:0000256|HAMAP-Rule:MF_00046}.
ACT_SITE 1069 1069 {ECO:0000256|HAMAP-Rule:MF_00037}.
ACT_SITE 1120 1120 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00037}.
ACT_SITE 1210 1210 {ECO:0000256|HAMAP-Rule:MF_00037}.
BINDING 20 20 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 169 169 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 175 175 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 177 177 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOD_RES 209 209 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 1220 AA; 134331 MW; 33C075245BBD9AE3 CRC64;
MQLEELLQKI GNYSGITDDS RKVMKNYIFV AIRGIKNDGH DFISDALKNG AGVVVGEEEI
KISIPYLKVL DSREALGKLA SHFFGNPSNR LKVIGVTGTD GKTTTANLIY FMLETAGKRV
GLISTLGAKI DKEEVDTGLH VTNPDPISLQ KILSEFVLKG AEFAVVEVTS HGLDQKRVAG
VKFDMGVLTN ITREHLDYHK TFEAYVKAKS KLFAGVRISV LNKNDSSYKK IKPLIPKGIK
IIEYPMALSG PLVEATNGRF PEDYNKLNTQ AAIAAVRVFV DFAHTPNALQ NALFELRKKV
GRKGKIISVF GSAGERDRAK RSIMGEISAR LADVSVFTAE DPRSEDVEGI IDQLVEGTKK
VKGEPKYYRI SERGEAIWFA VNKLAGSEDI VAIFGKGHEK SMAYGVKEYP WSDQEAVYEA
LKGRIKLVEK GFDFDRLKNV HFTGIKGVGM ASLALCFDDL GIKVSGSDTN EVFVTDETLE
KRKISWRVGF SGKNVSRKCD LLITTGAHGG LTNPEVLEAK KRGIATITHA EGLAKIGAGK
EVIAVSGVGG KSTTSSIISH LLEKAGLEPS FAIGVGNIFP LGTPGKFNSK GKHFICEADE
FAISPGINDN PRFSLLSPKI LVATNIEHDH PDIYPRLSDT KETFKEFFKK VPEDGWLVVN
VDNKNIRDVI SDVDVPKATY GFSPDADWKI FDVSYSPGST LFSLIHRGDI VKNMKINIPG
QYNVQNATAA FVVATLLGIS PKKVKDGLNS FVGVKRRFEF VGEVGGMLIY DDYAHHPLEI
KAVLKAARQW FPDRRVVAVF QPHTYSRTKA LFGQFAESFK GANVSAFMDI YSSAREKKDP
NVSSERLAQE TKKYVKNSYY IGSHKEATYW LKKNLRSGDL LLTLGAGDIF YLHEDLLGKT
KAINEPKSIF GDKVLSQEPL ENHTTLGLGG PASFFIKADS EDELISIVKK ANSLGVKNMV
IGDGSDLLVS EKGFPGLVIK NNIQGIKTSN YKFMVKCGTS LQSLVDRSIM EGCQGMEKMT
GIPGTVGGAV YGNAGAYGQV VSDNLTRVRA FDGKKVRWVP KKLCQFGYRE SIFKKNKWVL
LEVEFLFKSK VSPAQLKKEA ADTLTLRLKK YKPGLKCPGS FFKNIEVKDL TREQLIKIPK
EKIVYGKIPA GYLLEEVGAK GKRLGKILIA DFHANLFINT GGGNPTDFYK LAKTYTKKVE
EKFGIKLEPE VQLVGFSQNV


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