ID I4A995_DESDJ Unreviewed; 361 AA. AC I4A995; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 24-JAN-2024, entry version 61. 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=Desde_2184 {ECO:0000313|EMBL:AFM00530.1}; OS Desulfitobacterium dehalogenans (strain ATCC 51507 / DSM 9161 / JW/IU-DC1). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae; OC Desulfitobacterium. OX NCBI_TaxID=756499 {ECO:0000313|EMBL:AFM00530.1, ECO:0000313|Proteomes:UP000006053}; RN [1] {ECO:0000313|Proteomes:UP000006053} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51507 / DSM 9161 / JW/IU-DC1 RC {ECO:0000313|Proteomes:UP000006053}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T., RA de Vos W.M., Smidt H., Woyke T.; RT "Complete sequence of Desulfitobacterium dehalogenans ATCC 51507."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFM00530.1, ECO:0000313|Proteomes:UP000006053} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51507 / DSM 9161 / JW/IU-DC1 RC {ECO:0000313|Proteomes:UP000006053}; RX PubMed=25512312; DOI=10.1128/JB.02370-14; RA Kruse T., van de Pas B.A., Atteia A., Krab K., Hagen W.R., Goodwin L., RA Chain P., Boeren S., Maphosa F., Schraa G., de Vos W.M., van der Oost J., RA Smidt H., Stams A.J.; RT "Genomic, proteomic, and biochemical analysis of the organohalide RT respiratory pathway in Desulfitobacterium dehalogenans."; RL J. Bacteriol. 197:893-904(2015). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + CC phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, CC ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4; CC Evidence={ECO:0000256|HAMAP-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|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; CP003348; AFM00530.1; -; Genomic_DNA. DR RefSeq; WP_014794016.1; NC_018017.1. DR AlphaFoldDB; I4A995; -. DR STRING; 756499.Desde_2184; -. DR KEGG; ddh:Desde_2184; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_0_9; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000006053; 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: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; 3.40.50.20; -; 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 PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1. DR PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 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|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}. FT DOMAIN 140..345 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 312 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 312 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 314 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 361 AA; 40016 MW; 8C34B465AF5F71C7 CRC64; MTRQKIIILF GGQSGEHEVS LNSASSVLKA IDKEKYEVET LGISKSGQWH WGIRPEQWQQ DPTLQGILVN LVHDPSNPRF IALDGSTLPQ DGTFDLIFPV LHGPFGEDGT IQGLFEMANI PYAGSGVLGS ALGMDKDRMK AVFTEAGLPQ APYLTVLRTT LQKMMEKVLH DIEHSLGYPC FVKPANLGSS VGISKARNRE ELINALHLAA EYDRKIVVEQ NIVGREIELS VLGNEDAKAS IPGEILPSKD FYDYEAKYID TGSRLVIPAP LDQEVVKSLQ EKAVAAFKAV EACGLSRVDF FVTEGNQIYI NEINTMPGFT QISMYPKLWE ASGIPYSELI TQLIELGFQR FRDSRSRKIS L //