ID M2ZH99_9PSEU Unreviewed; 354 AA.
AC M2ZH99;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:EME60298.1};
GN ORFNames=H074_14767 {ECO:0000313|EMBL:EME60298.1};
OS Amycolatopsis decaplanina DSM 44594.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1284240 {ECO:0000313|EMBL:EME60298.1, ECO:0000313|Proteomes:UP000054226};
RN [1] {ECO:0000313|EMBL:EME60298.1, ECO:0000313|Proteomes:UP000054226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44594 {ECO:0000313|EMBL:EME60298.1,
RC ECO:0000313|Proteomes:UP000054226};
RX PubMed=23558534;
RA Kaur N., Kumar S., Bala M., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Amycolatopsis decaplanina Strain DSM 44594T.";
RL Genome Announc. 1:E0013813-E0013813(2013).
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}.
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:EME60298.1}.
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DR EMBL; AOHO01000048; EME60298.1; -; Genomic_DNA.
DR RefSeq; WP_007030851.1; NZ_AOHO01000048.1.
DR AlphaFoldDB; M2ZH99; -.
DR PATRIC; fig|1284240.4.peg.3005; -.
DR OrthoDB; 9804753at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000054226; Unassembled WGS sequence.
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; 3.30.465.10; -; 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 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.
DR PROSITE; PS51387; FAD_PCMH; 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}.
FT DOMAIN 21..186
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 346
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ SEQUENCE 354 AA; 37029 MW; 4BAE976C08D1BAF4 CRC64;
MSTAETPTQH AALADHTTLR LGGPARRYAE AKTVQALVDA VREADEAGEP VLLLGGGSNL
VVADDGFEGA VLKVGNTGWT RDGDLVEVAA GQNWDGFVEG LVAEGVGGLE CLSGIPGSVG
ATPIQNVGAY GCEVAESLVS VDLYDRAGRE IRTLTAEELG FGYRTSILKG TDAGIVLTVR
FKVTEDGLSA PIRYAELART LGVEIGDRVP AAEAREAVLR LRRGKGMVLD ADDHDTWSAG
SFFTNPIIGE ARLAKVLAGI VDVVGEDVRV PQYPAPGGTK LSAAWLIERA GFGKGHEGPG
GRVSLSTKHT LALTNRGKAS TEDLLALARE VRDGVEARFG VSLHPEPLLI NCSL
//
