ID E6MLT1_9BACT Unreviewed; 251 AA.
AC E6MLT1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|HAMAP-Rule:MF_00037};
DE EC=1.3.1.98 {ECO:0000256|HAMAP-Rule:MF_00037};
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00037};
GN Name=murB {ECO:0000256|HAMAP-Rule:MF_00037,
GN ECO:0000313|EMBL:EFV05406.1};
GN ORFNames=HMPREF9420_0448 {ECO:0000313|EMBL:EFV05406.1};
OS Segatella salivae DSM 15606.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV05406.1, ECO:0000313|Proteomes:UP000003874};
RN [1] {ECO:0000313|EMBL:EFV05406.1, ECO:0000313|Proteomes:UP000003874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV05406.1,
RC ECO:0000313|Proteomes:UP000003874};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-
CC Rule:MF_00037}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV05406.1}.
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DR EMBL; AEQO01000045; EFV05406.1; -; Genomic_DNA.
DR AlphaFoldDB; E6MLT1; -.
DR STRING; 888832.HMPREF9420_0448; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_0_0_10; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003874; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide 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 HAMAP; MF_00037; MurB; 1.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000003874}.
FT DOMAIN 10..65
FT /note="FAD linked oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01565"
FT DOMAIN 129..250
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02873"
FT ACT_SITE 77
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 247
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ SEQUENCE 251 AA; 28676 MW; C096621AFD066D9D CRC64;
MVLESFFDNI VDYAVAHRYY GLENLSLIPG EVGASAVQNI GAYGVEIKDF IHSIEAVEIE
SGKLICFSNE DCQYGYRQSK FKHEWRDKYL ITAVTYRLSS LFESHLDYGN IKIKLVEKQI
EKPTAEQLRN IIIEIRQEKL PDPKVTGNAG SFFMNPIVDE KKHKQLLSDY PQMPFYRVSQ
NEYKIPAGWM IEQCGWKGKA LGKAAVHDKQ ALVLINLGGA TGKDIVTLCE TIQRDVQKRF
GIWINPEVNI R
//
