ID J5KBI2_9GAMM Unreviewed; 327 AA.
AC J5KBI2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:EJP72658.1};
GN ORFNames=NT02SARS_1119 {ECO:0000313|EMBL:EJP72658.1};
OS SAR86 cluster bacterium SAR86B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1123867 {ECO:0000313|EMBL:EJP72658.1, ECO:0000313|Proteomes:UP000010116};
RN [1] {ECO:0000313|EMBL:EJP72658.1, ECO:0000313|Proteomes:UP000010116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT lineage.";
RL ISME J. 6:1186-1199(2012).
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; JH611190; EJP72658.1; -; Genomic_DNA.
DR AlphaFoldDB; J5KBI2; -.
DR HOGENOM; CLU_035304_0_0_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010116; 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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR HAMAP; MF_00037; MurB; 1.
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.
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:UP000010116}.
FT DOMAIN 25..137
FT /note="FAD linked oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01565"
FT DOMAIN 207..326
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02873"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 322
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ SEQUENCE 327 AA; 37142 MW; 28E6C60FEB7FB981 CRC64;
MKINKDHQII NSLRISSHSK YNFLIENNND CHELYDFIRL KRLPYIVIGE GTNIVAPEYF
NGIVIQISLN NINNDKHLNV GASANWNELV EYTIKKNIYG FENLSLIPGS VGAAPVQNIG
AYGVEISSLI KSVECFDLSN NSFITINGSD CNFKYRHSCF KDNPDLLILS VNFFNNLKKE
FNLNYDSITS YINENNIDFN NLEHNEVAEI INTIRSSKLP DPNNIPNVGS FFKNPIIDNS
RLSEFNNFIS WPVTDNSSKL SAGQLIGSIK HLLPSYENVD LYEHHSLVMI TNSKASYEEV
LDFKNSISKT IFNNYSIHLD VEPTIIT
//
