MURB_LEPIC
ID MURB_LEPIC Reviewed; 318 AA.
AC Q72MQ5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 25-MAY-2022, entry version 107.
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=LIC_13138;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS71683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016823; AAS71683.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001978935.1; NC_005823.1.
DR AlphaFoldDB; Q72MQ5; -.
DR SMR; Q72MQ5; -.
DR PaxDb; Q72MQ5; -.
DR EnsemblBacteria; AAS71683; AAS71683; LIC_13138.
DR GeneID; 61143010; -.
DR KEGG; lic:LIC_13138; -.
DR HOGENOM; CLU_035304_1_1_12; -.
DR OMA; MQNIGAY; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007037; Chromosome I.
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; 3.30.43.10; -; 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.
FT CHAIN 1..318
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179223"
FT DOMAIN 38..204
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT REGION 212..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 233
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ SEQUENCE 318 AA; 35324 MW; 7AE86D822589A390 CRC64;
MSPVLSESQL RDFKHTLESS KIPFRSEVRL GILSSFKIGG VCPVIVEPEI SSQVSEILHI
FSKFDIPWKI LGGGSNLLIS DHPDNFVTLR LSGKFKEFVS LGDGKFKIGA ATNTTPTFRQ
ISQLGYTGAE FLSTIPGWTG GAVIQNAGCY GGELFDLIES VEFLRNGEVF VRKPSEIKYG
YRFTEFLNQK DSIILGIEIL LKEGNLEEIE SSLKDKRDRR NSSQPENKKS AGSVFKNPKV
FREDGKEIKA WELLDQAGLR GQIKGGAQIS PEHCNFIVNL GTATASDVHY LIDLVVDRVY
QTSGILLNRE IEFFGDIP
