ID E4TFX7_CALNY Unreviewed; 416 AA. AC E4TFX7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}; DE EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}; 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=Calni_1727 {ECO:0000313|EMBL:ADR19633.1}; OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1). OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales; OC Calditerrivibrionaceae. OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR19633.1, ECO:0000313|Proteomes:UP000007039}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672; 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., Ivanova N., Mikhailova N., Zeytun A., RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Calditerrivibrio nitroreducens DSM RT 19672."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADR19633.1, ECO:0000313|Proteomes:UP000007039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1 RC {ECO:0000313|Proteomes:UP000007039}; RX PubMed=21475587; DOI=10.4056/sigs.1523807; RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Land M.; RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain RT (Yu37-1)."; RL Stand. Genomic Sci. 4:54-62(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|HAMAP-Rule:MF_00639, CC 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. {ECO:0000256|HAMAP- CC Rule:MF_00639}. 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; CP002347; ADR19633.1; -; Genomic_DNA. DR RefSeq; WP_013451844.1; NC_014758.1. DR AlphaFoldDB; E4TFX7; -. DR STRING; 768670.Calni_1727; -. DR KEGG; cni:Calni_1727; -. DR eggNOG; COG0771; Bacteria. DR HOGENOM; CLU_032540_0_0_0; -. DR OrthoDB; 9809796at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000007039; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro. 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 HAMAP; MF_00639; MurD; 1. DR InterPro; IPR018109; Folylpolyglutamate_synth_CS. 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 SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1. DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1. DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 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|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:UP000007039}. FT DOMAIN 88..185 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 274..341 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT BINDING 90..96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639" SQ SEQUENCE 416 AA; 46826 MW; 1DA6835077503310 CRC64; MKAAILGYGK SGQTAKRLLE IKGTETIEIY DDKMDGFKGI KDFNYEEFDT VVVSPGIDLT NIDLPTERIT SELELAFEFI KDKKIIGITG TNGKSTVTFL TAQLLKNIGI NAEFCGNIGV TVGDTYLLKN PDVYVVEVSS FQLDLLKRFR FDTSTITNIT PDHLDRYKTM DRYITSKSRM VEFTEGVSFL EKGGWNEIFK KYENIKYVDG ELKSYPLLNG NLLEFEDFYV DVNRYNLFGF HNIVNLSFAL LLTNQIVRLK GDVTGLVENL TPLEHRCELV TEINGVKYIN DSKGTNVDST LTALKSSSYP TTLILGGKDK NGDFSVLSDE INKKAKLVIC CGAAGEKIYN SLKDIIDVKI VRVELLKDAI SLAYRETKEG TVLFSPACAS FDEFNNFEER GRFFKNYVNN LKVRGC //