MURB_THET8
ID MURB_THET8 Reviewed; 265 AA.
AC Q5SJC8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
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}; OrderedLocusNames=TTHA1086;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-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}.
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; AP008226; BAD70909.1; -; Genomic_DNA.
DR RefSeq; WP_011228429.1; NC_006461.1.
DR RefSeq; YP_144352.1; NC_006461.1.
DR PDB; 2GQT; X-ray; 1.30 A; A=1-265.
DR PDB; 2GQU; X-ray; 1.60 A; A=1-265.
DR PDBsum; 2GQT; -.
DR PDBsum; 2GQU; -.
DR AlphaFoldDB; Q5SJC8; -.
DR SMR; Q5SJC8; -.
DR STRING; 300852.55772468; -.
DR EnsemblBacteria; BAD70909; BAD70909; BAD70909.
DR GeneID; 3168182; -.
DR KEGG; ttj:TTHA1086; -.
DR PATRIC; fig|300852.9.peg.1066; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_1_1_0; -.
DR OMA; MQNIGAY; -.
DR PhylomeDB; Q5SJC8; -.
DR BRENDA; 1.3.1.98; 6330.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q5SJC8; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..265
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000224733"
FT DOMAIN 15..169
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT REGION 182..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:2GQT"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2GQT"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:2GQT"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:2GQT"
SQ SEQUENCE 265 AA; 29180 MW; A61870724DA500A2 CRC64;
MRVERVLLKD YTTLGVGGPA ELWTVETREE LKRATEAPYR VLGNGSNLLV LDEGVPERVI
RLAGEFQTYD LKGWVGAGTL LPLLVQEAAR AGLSGLEGLL GIPAQVGGAV KMNAGTRFGE
MADALEAVEV FHDGAFHVYC PEELGFGYRK SHLPPGGIVT RVRLKLKERP KEEILRRMAE
VDRARKGQPK RKSAGCAFKN PPGQSAGRLI DERGLKGLRV GDAMISLEHG NFIVNLGQAR
AKDVLELVRR VQEELPLELE WEVWP
