ID A6V3C1_PSEA7 Unreviewed; 339 AA.
AC A6V3C1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|ARBA:ARBA00015188, ECO:0000256|HAMAP-Rule:MF_00037};
DE EC=1.3.1.98 {ECO:0000256|ARBA:ARBA00012518, ECO:0000256|HAMAP-Rule:MF_00037};
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|ARBA:ARBA00031026, ECO:0000256|HAMAP-Rule:MF_00037};
GN Name=murB {ECO:0000256|HAMAP-Rule:MF_00037,
GN ECO:0000313|EMBL:ABR82059.1};
GN OrderedLocusNames=PSPA7_2184 {ECO:0000313|EMBL:ABR82059.1};
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR82059.1, ECO:0000313|Proteomes:UP000001582};
RN [1] {ECO:0000313|EMBL:ABR82059.1, ECO:0000313|Proteomes:UP000001582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7 {ECO:0000313|EMBL:ABR82059.1,
RC ECO:0000313|Proteomes:UP000001582};
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR82059.1, ECO:0000313|Proteomes:UP000001582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7 {ECO:0000313|EMBL:ABR82059.1,
RC ECO:0000313|Proteomes:UP000001582};
RX PubMed=20107499; DOI=10.1371/journal.pone.0008842;
RA Roy P.H., Tetu S.G., Larouche A., Elbourne L., Tremblay S., Ren Q.,
RA Dodson R., Harkins D., Shay R., Watkins K., Mahamoud Y., Paulsen I.T.;
RT "Complete genome sequence of the multiresistant taxonomic outlier
RT Pseudomonas aeruginosa PA7.";
RL PLoS ONE 5:E8842-E8842(2010).
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921,
CC ECO:0000256|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:0000256|ARBA:ARBA00001501, ECO:0000256|HAMAP-
CC Rule:MF_00037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00037};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00037}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|ARBA:ARBA00010485,
CC ECO:0000256|HAMAP-Rule:MF_00037}.
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DR EMBL; CP000744; ABR82059.1; -; Genomic_DNA.
DR RefSeq; WP_012075166.1; NC_009656.1.
DR AlphaFoldDB; A6V3C1; -.
DR KEGG; pap:PSPA7_2184; -.
DR HOGENOM; CLU_035304_0_0_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase 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 Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.90.78.10; UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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 NCBIfam; TIGR00179; murB; 1.
DR PANTHER; PTHR21071; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1.
DR PANTHER; PTHR21071:SF4; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF02873; MurB_C; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56194; Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00037};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00037};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00037};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00037};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00037}.
FT DOMAIN 18..189
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 166
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 335
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ SEQUENCE 339 AA; 37371 MW; 1DD5A36B41255699 CRC64;
MSLELQEQCS LKPYNSFGID VRARLLAHAH GEADVREALA LARQRSLPLL VIGGGSNLLL
TRDVEALVLR MASQGRRILS EADDMVLVEA EAGETWDPFV QWSLEQGLAG LENLSLIPGT
VGAAPMQNIG AYGVELKDVF DSLTALDRQD GSLREFDREA CRFGYRDSLF KQEPDRWLIL
RVRLRLSRRS GLHLDYGPVR QRLQEEGIAN PTAQDVSRVI CAIRREKLPD PAVLGNAGSF
FKNPLVSATQ AAMLRRTYPD LVAYPQADGQ VKLAAGWLID KGGWKGFRDG PVGVHAQQAL
VLVNHGGASG AQVQALAERI QADVRQRFGV ELEREPNLY
//