ID   MURB1_CORGL             Reviewed;         335 AA.
AC   Q8NTF4;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase 1;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase 1;
GN   Name=murB1; Synonyms=murB; OrderedLocusNames=Cgl0353, cg0423;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}.
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DR   EMBL; BA000036; BAB97746.1; -; Genomic_DNA.
DR   EMBL; BX927149; CAF19067.1; -; Genomic_DNA.
DR   RefSeq; NP_599604.1; NC_003450.3.
DR   RefSeq; WP_011013593.1; NC_006958.1.
DR   AlphaFoldDB; Q8NTF4; -.
DR   SMR; Q8NTF4; -.
DR   STRING; 196627.cg0423; -.
DR   PRIDE; Q8NTF4; -.
DR   KEGG; cgb:cg0423; -.
DR   KEGG; cgl:Cgl0353; -.
DR   PATRIC; fig|196627.13.peg.356; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_1_11; -.
DR   OMA; KMNAGMK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000582; Chromosome.
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; Reference proteome.
FT   CHAIN           1..335
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase 1"
FT                   /id="PRO_0000179203"
FT   DOMAIN          36..202
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        231
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  36371 MW;  72EFABF86B66D56E CRC64;
     MNDFKKVSES LETALRNEFD FRFATEVSLK EISRWRIGGP AAVFAEPSSI NEICALLAFM
     KNRPEPVVVV GGTSNILFDS DGFGGLVIKL GENFSNFIIE GSRIRAQAGA SVPQLVRAVA
     TEGLEGIVHA GGIPGTVGGL VVMNGGTQRR GIGEHVTKVL VTDAEGSIRE LNANELQFTY
     RNSVLKNSET TVLEVELLLK PGNAGELLAE LETILDQRSQ KFPEDLPNCG STFLSDPAMY
     SIVGPPGKAI EDAGLKGLRR GSAEISMQHA NFIVNHGDAS DDDILWLISA VRKEVYSRTG
     FVMDCEVLYL SYSGDFRPAH EVADEQWPDI DLVRN