ID   MURB_BARBK              Reviewed;         324 AA.
AC   A1UTC3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   04-NOV-2026, entry version 103.
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=BARBAKC583_0945;
OS   Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / KC583 / Herrer 020/F12,63;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3-O-(1-
CC         carboxyvinyl)-alpha-D-glucosamine + NADPH + H(+);
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CP000524; ABM44449.1; -; Genomic_DNA.
DR   SMR; A1UTC3; -.
DR   STRING; 360095.BARBAKC583_0945; -.
DR   KEGG; bbk:BARBAKC583_0945; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_0_5; -.
DR   OMA; AACEFGY; -.
DR   UniPathway; UPA00219; -.
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; 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; 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.
DR   NCBIfam; NF010480; murB; 1.
DR   NCBIfam; TIGR00179; murB; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0071555; P:cell wall organization; IEA:TreeGrafter.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   AlphaFoldDB; A1UTC3; -.
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..324
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_1000002863"
FT   DOMAIN          39..220
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        234
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ   SEQUENCE   324 AA;  35898 MW;  79D4192C6A743B68 CRC64;
     MNFQPIDGKK LLAWLQPVLS DIKGKITPNV EMRKVTWFRT GGLAELFYQP ADEDDLALFF
     KVLPEFVPVT IVGIGSNLLV RDGGIPGVVI RLSTKSFGQI KQVSSTRFLV GAATADKHLA
     SAALEAEISG FHFYHGIPGG LGGALKMNAG ANGVETAERV VEVYALDRKG ERHILNLRDM
     NYAYRHCNIP EGLVFTAALL EGDVGNKDDI RAAMHEVALH RETVQPIREK TGGSTFRNLE
     DISAWKVIDE AGCRGLQIGG AQMSEMHCNF MINMGEATGY DLEKLGETVR ARVFNHSAHH
     LEWEIQRIGQ FEQDRIVLPF DQFH
//