ID C9RDA7_AMMDK Unreviewed; 308 AA. AC C9RDA7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 02-SEP-2026, entry version 90. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047}; GN Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; GN OrderedLocusNames=Adeg_1108 {ECO:0000313|EMBL:ACX52234.1}; OS Ammonifex degensii (strain DSM 10501 / KC4). OC Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Ammonifex. OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52234.1, ECO:0000313|Proteomes:UP000002620}; RN [1] {ECO:0000313|EMBL:ACX52234.1, ECO:0000313|Proteomes:UP000002620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620}; RG US DOE Joint Genome Institute; RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A., RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.; RT "Complete sequence of chromosome of Ammonifex degensii KC4."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 D-alanine + ATP = D-alanyl-D-alanine + ADP + phosphate + CC H(+); Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822, CC ChEBI:CHEBI:456216; EC=6.3.2.4; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00047}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR039102-3}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}. 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; CP001785; ACX52234.1; -; Genomic_DNA. DR RefSeq; WP_015739111.1; NC_013385.1. DR AlphaFoldDB; C9RDA7; -. DR STRING; 429009.Adeg_1108; -. DR KEGG; adg:Adeg_1108; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_2_0_9; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002620; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.30.470.20:FF:000008; D-alanine--D-alanine ligase; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR000291; D-Ala_lig_Van_CS. DR InterPro; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR011127; Dala_Dala_lig_N. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1. DR NCBIfam; NF002378; PRK01372.1; 1. DR NCBIfam; NF002528; PRK01966.1-4; 1. DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1. DR PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00047}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00047}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00047}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039102-3}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR039102-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR039102-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00047}; Reference proteome {ECO:0000313|Proteomes:UP000002620}. FT DOMAIN 99..301 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT ACT_SITE 13 FT /evidence="ECO:0000256|PIRSR:PIRSR039102-1" FT ACT_SITE 145 FT /evidence="ECO:0000256|PIRSR:PIRSR039102-1" FT ACT_SITE 279 FT /evidence="ECO:0000256|PIRSR:PIRSR039102-1" FT BINDING 255 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 308 AA; 34121 MW; 3307237EEA2F773F CRC64; MRVAVLCGGN SAEREVSLRS GEAVYRALQE RGWEAVKIDV GPDIALRLSE VKPDVVFLAL HGKGGEDGSI QGLLEVMGLP YTGPGILASA LAMNKIATKR YLRSASLPTP DFITLDKEET HDEWLQRVKE FRPFPVVVKA PTQGSSLGMN IVRREEELLP ALAEAFRYDP VVLVEEFIEG VEVTAAVLGN RKPVVLPLIE IVADKGVYDY EAKYTPGKSQ HIIPPRLPEP WQEKVKELAL ATYRWLDCRG FSRIDFMVDH KGNPYILEVN TIPGLTEVSL FPDAARAAGI SFGELVERLI YLALGREE //