UniProt: B0PDT1

Database: UniProt
Entry: B0PDT1_9FIRM

LinkDB:  B0PDT1_9FIRM 
Original site:  B0PDT1_9FIRM

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
All databases (23)   

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ID   B0PDT1_9FIRM            Unreviewed;       303 AA.
AC   B0PDT1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
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:EDS10120.1};
GN   ORFNames=ANACOL_02716 {ECO:0000313|EMBL:EDS10120.1};
OS   Anaerotruncus colihominis DSM 17241.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS10120.1, ECO:0000313|Proteomes:UP000003803};
RN   [1] {ECO:0000313|EMBL:EDS10120.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10120.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS10120.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10120.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2007) 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:EDS10120.1}.
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DR   EMBL; ABGD02000024; EDS10120.1; -; Genomic_DNA.
DR   RefSeq; WP_006875620.1; NZ_DS544185.1.
DR   AlphaFoldDB; B0PDT1; -.
DR   STRING; 169435.ERS852551_00865; -.
DR   GeneID; 72465646; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_1_9; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000003803; 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          32..199
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        228
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   303 AA;  32665 MW;  4D468A0304659F25 CRC64;
     MNAIAQLRKD CERIGCICLA DEPMAAHTSF KIGGPADLLL KPRDAETAAR VIARARELSV
     PLLFIGKGSD LLICDEGVRG AVLSFDEASA RPSLRDETVI DCPAGASLTA LCCFALEQGL
     TGLEFAYGIP GSVGGAVYMN AGAYGGEIRD VVGSVRFLDG QGKLRALEEC ALELSYRHSY
     FTDHPDCLIT SASFHLRRGD RDAIRARMDD LMERRRTKQP LEYPSAGSTF KRPKGAYASA
     LIDGCGLKGR RVGGAMVSEK HAGFVINYDN ASCTDVLTLI GEIQTQVREQ TGFSLECEVK
     YIG
//

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