ID F3ZZ21_MAHA5 Unreviewed; 452 AA.
AC F3ZZ21;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|ARBA:ARBA00015655, ECO:0000256|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000256|ARBA:ARBA00012212, ECO:0000256|HAMAP-Rule:MF_00639};
DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN Name=murD {ECO:0000256|HAMAP-Rule:MF_00639};
GN OrderedLocusNames=Mahau_1592 {ECO:0000313|EMBL:AEE96780.1};
OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE96780.1, ECO:0000313|Proteomes:UP000008457};
RN [1] {ECO:0000313|Proteomes:UP000008457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC {ECO:0000313|Proteomes:UP000008457};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R.,
RA Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Mahella australiensis DSM 15567.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEE96780.1, ECO:0000313|Proteomes:UP000008457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC {ECO:0000313|Proteomes:UP000008457};
RX PubMed=21886860;
RA Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M.,
RA Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Mahella australiensis type strain (50-1
RT BON).";
RL Stand. Genomic Sci. 4:331-341(2011).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001059, ECO:0000256|HAMAP-
CC Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639,
CC ECO:0000256|RuleBase:RU003664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC -!- SIMILARITY: Belongs to the MurCDEF family.
CC {ECO:0000256|ARBA:ARBA00010416, ECO:0000256|HAMAP-Rule:MF_00639}.
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DR EMBL; CP002360; AEE96780.1; -; Genomic_DNA.
DR RefSeq; WP_013781209.1; NC_015520.1.
DR AlphaFoldDB; F3ZZ21; -.
DR STRING; 697281.Mahau_1592; -.
DR KEGG; mas:Mahau_1592; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_0_0_9; -.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008457; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase 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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
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 HAMAP; MF_00639; MurD; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR NCBIfam; TIGR01087; murD; 1.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF21799; MurD-like_N; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00639};
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00639};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00639};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00639};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Reference proteome {ECO:0000313|Proteomes:UP000008457}.
FT DOMAIN 113..291
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 311..379
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 115..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 452 AA; 49688 MW; D1E0EF6AB47DF8C5 CRC64;
MELKDKRILI IGMALSGIAA AKVLYRHGAH IILNDIKEQC ELGDALNQLE GIKAEYAFGA
EPDELLERCD MAIVSPGVPF DKPFVKKARS LGIELIGEVE LAYRLSNVPI AAITGTNGKT
TTTALTGHIF KLAGVNTFVC GNIGMPMISA IEQYGPGDVV VAEISSFQLE SIRYFKPHVS
AILNITEDHL NRHGTFDNYI AIKSRIFMNQ GPDDYVVLNM DNEPCRQLIE LPNAHVLPFS
RKQELDEGAM VKDNYIICRL NSREDKICRV NDIKIPGKHN LENALASAAI AYAMGIGPDV
IAQGLRTFEG VEHRIEFVDE IDGVRFINDS KGTNPDAAVK AIEAVDGPII LIAGGMDKHA
DFTGFIEAFD SKVKALVLLG ETADQIASAA RRMGFDNIYK VHSLQEAVEQ AWHLSSAGDC
ILLSPACASW DMFDNFEQRG MVFKEAVRKL RR
//
