ID E6J9U2_9ACTN Unreviewed; 308 AA.
AC E6J9U2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000313|EMBL:EFV91633.1};
DE EC=6.3.2.9 {ECO:0000313|EMBL:EFV91633.1};
DE Flags: Fragment;
GN Name=murD {ECO:0000313|EMBL:EFV91633.1};
GN ORFNames=ES5_09972 {ECO:0000313|EMBL:EFV91633.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV91633.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV91633.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV91633.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV91633.1}.
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DR EMBL; AEKG01000202; EFV91633.1; -; Genomic_DNA.
DR AlphaFoldDB; E6J9U2; -.
DR Proteomes; UP000004165; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFV91633.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 18..67
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|Pfam:PF01262"
FT DOMAIN 162..279
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT NON_TER 308
FT /evidence="ECO:0000313|EMBL:EFV91633.1"
SQ SEQUENCE 308 AA; 30935 MW; CB4CD6138162F6F8 CRC64;
MTETTPTTGA AAGRDLDVRE LAGTRVLVLG AGVSGPGAVR ILDALGAEPV VADSRPEAIA
RLREALPDGV ACEGVDLDRA AELLAASRGP VGQAGGAGGA GAAGAVDRIG IDLVVTSPGW
RPDSPLLVAA ADAGIAVWGD VELAWRADAA ELFGPRRTWL AVTGTNGKTT TTSMLEAICL
EAGMAARACG NIGLPVTDVL LAEPRVEVLA AELSSFQLHW APSCRPDVGV VLNVAEDHLD
WHGSMEAYAA AKAQVLTGRV AVAGADDEIA ARLLADAPAA TRIGVRLGAP AAGECGVVDG
VLTARIGG
//
