ID A0A139BWU1_9PROT Unreviewed; 326 AA.
AC A0A139BWU1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ORFNames=AWT59_0545 {ECO:0000313|EMBL:KXS33383.1};
OS Candidatus Gallionella acididurans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Gallionella.
OX NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS33383.1, ECO:0000313|Proteomes:UP000070578};
RN [1] {ECO:0000313|EMBL:KXS33383.1, ECO:0000313|Proteomes:UP000070578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33383.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXS33383.1, ECO:0000313|Proteomes:UP000070578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33383.1};
RA Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E.,
RA Pimenov N., Karnachuk O., Ravin N.;
RT "New uncultured bacterium of the family Gallionellaceae from acid mine
RT drainage: description and reconstruction of genome based on metagenomic
RT analysis of microbial community.";
RL Submitted (MAR-2016) 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:KXS33383.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSLI01000007; KXS33383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139BWU1; -.
DR PATRIC; fig|1796491.3.peg.594; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000070578; 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}; Reference proteome {ECO:0000313|Proteomes:UP000070578}.
FT DOMAIN 32..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 317
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ SEQUENCE 326 AA; 35178 MW; 2D404CFAEE398C6C CRC64;
MNMTELQHYA KSPLRGTLSR DEPMRKHTSW RTGGTAERMY QPADLEDLLV FLRGLPPDEP
LCAVGLGSNL LVRDGGLRGT VLLLHGSLSA LHLEMDGSIY AEAGVPGAKL ARFAAQHNLQ
GAEFFAGIPG TLGGMLAMNA GCYGSETWEK VMRVQTVDRR GEVHVRTPAE YEIGYRHVIR
TEGKGLGAGE DPHVLQSSVL SPQSSEFFVA AWLQLARGDG DEARLGIKAL LSKRIATQPL
NLPNAGSVFR NPPGDHAARL IEQCGLKGRQ IGGAQVSEKH ANFIVNLGAA SAADIENLIL
EVQAEVQQQT GVKLHPEVRI VGEMRS
//
