MURB_SHESR
ID MURB_SHESR Reviewed; 341 AA.
AC Q0I0C3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 89.
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};
GN OrderedLocusNames=Shewmr7_0176;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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=ABI41182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000444; ABI41182.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041417073.1; NC_008322.1.
DR AlphaFoldDB; Q0I0C3; -.
DR SMR; Q0I0C3; -.
DR EnsemblBacteria; ABI41182; ABI41182; Shewmr7_0176.
DR KEGG; shm:Shewmr7_0176; -.
DR HOGENOM; CLU_035304_0_0_6; -.
DR OrthoDB; 841869at2; -.
DR UniPathway; UPA00219; -.
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..341
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000332504"
FT DOMAIN 13..185
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 327
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ SEQUENCE 341 AA; 37077 MW; 46EB3303E76EE2B0 CRC64;
MSFPYSLKPF NTFGVEQSCL SMIEVHSKAE LQSTCLSLYQ SKRPMLVLGG GSNIVFTDDF
NGTVVRVLTK GISCSEDGTH FYLAVEAGEN WHELVQFSLN QNMPGLENLA LIPGTVGAAP
IQNIGAYGVE LCDICDWVEY LDLESGNLLR LTTDECEFAY RESIFKGSLR DKAVITAVGL
RLPKAWHPKL AYGPLQSFNA ETVTSREIFD RVCEVRSEKL PNPEELGNAG SFFKNPIVSA
ATYMQLAAHF PSIVGYAQPN GEVKLAAGWL IEHAGLKGFA LGNAGVHAKQ ALVLVNLGHA
TGQDICRLAL HVIARVNEVF GVKLEAEPRI MGLTGETSLD V