MURB_PSEAE
ID MURB_PSEAE Reviewed; 339 AA.
AC Q9HZM7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=PA2977;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG06365.1; -; Genomic_DNA.
DR PIR; A83274; A83274.
DR RefSeq; NP_251667.1; NC_002516.2.
DR RefSeq; WP_003106928.1; NZ_QZGE01000009.1.
DR PDB; 4JAY; X-ray; 2.23 A; A/B/C/D=1-339.
DR PDB; 4JB1; X-ray; 2.10 A; A=1-339.
DR PDB; 7OR2; X-ray; 2.35 A; A=3-339.
DR PDB; 7ORZ; X-ray; 1.85 A; A=3-339.
DR PDB; 7OSQ; X-ray; 2.07 A; A=1-339.
DR PDBsum; 4JAY; -.
DR PDBsum; 4JB1; -.
DR PDBsum; 7OR2; -.
DR PDBsum; 7ORZ; -.
DR PDBsum; 7OSQ; -.
DR AlphaFoldDB; Q9HZM7; -.
DR SMR; Q9HZM7; -.
DR STRING; 287.DR97_4962; -.
DR PaxDb; Q9HZM7; -.
DR PRIDE; Q9HZM7; -.
DR EnsemblBacteria; AAG06365; AAG06365; PA2977.
DR GeneID; 880517; -.
DR KEGG; pae:PA2977; -.
DR PATRIC; fig|208964.12.peg.3124; -.
DR PseudoCAP; PA2977; -.
DR HOGENOM; CLU_035304_0_0_6; -.
DR InParanoid; Q9HZM7; -.
DR OMA; MQNIGAY; -.
DR PhylomeDB; Q9HZM7; -.
DR BioCyc; PAER208964:G1FZ6-3029-MON; -.
DR BRENDA; 1.3.1.98; 5087.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..339
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179242"
FT DOMAIN 18..189
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 335
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4JAY"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:7ORZ"
FT TURN 121..128
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:7ORZ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 177..189
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:7ORZ"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7OR2"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:7ORZ"
FT HELIX 310..328
FT /evidence="ECO:0007829|PDB:7ORZ"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:7ORZ"
SQ SEQUENCE 339 AA; 37628 MW; C0C8EF9F2938FE27 CRC64;
MSLELQEHCS LKPYNTFGID VRARLLAHAR DEADVREALA LARERGLPLL VIGGGSNLLL
TRDVEALVLR MASQGRRIVS DAADSVLVEA EAGEAWDPFV QWSLERGLAG LENLSLIPGT
VGAAPMQNIG AYGVELKDVF DSLTALDRQD GTLREFDRQA CRFGYRDSLF KQEPDRWLIL
RVRLRLTRRE RLHLDYGPVR QRLEEEGIAS PTARDVSRVI CAIRREKLPD PAVLGNAGSF
FKNPLVDATQ AERLRQAFPD LVGYPQADGR LKLAAGWLID KGGWKGFRDG PVGVHAQQAL
VLVNHGGATG AQVRALAERI QEDVRRRFGV ELEPEPNLY
