ID J9GAN5_9ZZZZ Unreviewed; 338 AA.
AC J9GAN5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|ARBA:ARBA00012518};
DE EC=1.3.1.98 {ECO:0000256|ARBA:ARBA00012518};
GN ORFNames=EVA_13069 {ECO:0000313|EMBL:EJW98827.1};
OS gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=749906 {ECO:0000313|EMBL:EJW98827.1};
RN [1] {ECO:0000313|EMBL:EJW98827.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23251564; DOI=10.1371/journal.pone.0051521;
RA Alcaide M., Messina E., Richter M., Bargiela R., Peplies J., Huws S.A.,
RA Newbold C.J., Golyshin P.N., Simon M.A., Lopez G., Yakimov M.M., Ferrer M.;
RT "Gene sets for utilization of primary and secondary nutrition supplies in
RT the distal gut of endangered iberian lynx.";
RL PLoS ONE 7:E51521-E51521(2012).
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921}.
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};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EJW98827.1}.
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; AMCI01004084; EJW98827.1; -; Genomic_DNA.
DR AlphaFoldDB; J9GAN5; -.
DR UniPathway; UPA00219; -.
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-EC.
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-UniPathway.
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};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 17..188
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 338 AA; 37529 MW; 595DD3BF5FB9D8D2 CRC64;
MKEQTNFALQ AHHTFGMEVR AERFVEYASV AELKAFLADP SALSGRWLHI GGGSNLLFKG
DYQGTVLHSA IRGCEVVAED DTCVEVRVGA GVVWDDFVAE AVARGWYGAE NLSLIPGEVG
ASAVQNIGAY GVEAKDLIVR VETVEVATGA DRTFTNEECG YAYRQSCFKH ELKGKYIVTY
VTYRLQKQPV FHLDYGHVRE ELEKRGEEPT LDHVRRVIVA IRQDKLPDPK VQGNAGSFFM
NPVVPRAQFE ALLQLYPEMP HYEVDAERVK IPAAWMIDRC GWKGKRVGRA GVHDRQALVL
VNCGGATGEE VMALAGQIQA SVFERFGIHI SPEVNYIE
//
