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Database: UniProt
Entry: A0A0D6B4M4_RHOSU
LinkDB: A0A0D6B4M4_RHOSU
Original site: A0A0D6B4M4_RHOSU 
ID   A0A0D6B4M4_RHOSU        Unreviewed;       310 AA.
AC   A0A0D6B4M4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ECO:0000313|EMBL:BAQ70067.1};
GN   ORFNames=NHU_02920 {ECO:0000313|EMBL:BAQ70067.1};
OS   Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ70067.1, ECO:0000313|Proteomes:UP000064912};
RN   [1] {ECO:0000313|EMBL:BAQ70067.1, ECO:0000313|Proteomes:UP000064912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ70067.1,
RC   ECO:0000313|Proteomes:UP000064912};
RA   Nagao N.;
RT   "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL   Submitted (FEB-2015) 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}.
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DR   EMBL; AP014800; BAQ70067.1; -; Genomic_DNA.
DR   RefSeq; WP_060835429.1; NZ_AP014800.1.
DR   AlphaFoldDB; A0A0D6B4M4; -.
DR   KEGG; rsu:NHU_02920; -.
DR   PATRIC; fig|35806.4.peg.3001; -.
DR   eggNOG; COG0812; Bacteria.
DR   OMA; KMNAGMK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000064912; 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; 3.30.465.10; -; 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          24..187
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          201..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ   SEQUENCE   310 AA;  32621 MW;  5ABAB1BB98C8275D CRC64;
     MTQMPEPRGR LTPGKALSEL TWLRVGGPAD WLFQPADAED LATFLAALPA GMPVFPMGVG
     SNLIVRDGGI RGVVIRLGRG FNAISVAGAR VTAGAAALDA HVARRAAEAG VDLSFLRTIP
     GAIGGAVRMN AGCYGRYVAD VLVSARAVTR TGEIVTLSPG DLRLGYRQSH LPEGWVITEA
     TFEGRPGAPE ALAAQMEEQI ARRDASQPTR ARSAGSTFRN PAGFSSTGRA DDSHEMKAWS
     LIDAAGLRGA RRGGAQMSEK HSNFLINADG ATAADLEGLG EEVRKRVFQS SGIELEWEIL
     RVGEPAPGNP
//
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