ID D7AQL6_THEM3 Unreviewed; 325 AA. AC D7AQL6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 57. DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ADH59902.1}; DE EC=6.3.2.4 {ECO:0000313|EMBL:ADH59902.1}; GN OrderedLocusNames=Tmath_0117 {ECO:0000313|EMBL:ADH59902.1}; OS Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG OS 53645 / CIP 108742 / A3). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH59902.1, ECO:0000313|Proteomes:UP000002064}; RN [1] {ECO:0000313|EMBL:ADH59902.1, ECO:0000313|Proteomes:UP000002064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11426 / CIP 108742 / A3 RC {ECO:0000313|Proteomes:UP000002064}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.; RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii RT mathranii str. A3."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|ARBA:ARBA00010871}. 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; CP002032; ADH59902.1; -; Genomic_DNA. DR AlphaFoldDB; D7AQL6; -. DR STRING; 583358.Tmath_0117; -. DR KEGG; tmt:Tmath_0117; -. DR HOGENOM; CLU_039268_2_0_9; -. DR Proteomes; UP000002064; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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 InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR011095; Dala_Dala_lig_C. DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1. DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADH59902.1}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}. FT DOMAIN 105..316 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" SQ SEQUENCE 325 AA; 37177 MW; E1D790FF04FD031D CRC64; MKIGVLWRKF RNVEFQRKLM PDKVYDDAYD EAYHHYMAIK EAGFDSVLIE WKEDPLETYE TIKKEKVDLI FNASSMKEVA FLEVFNIPYV GSGLDLVATD KRMRKDIVAF HGLPTPKYVV AKNSQEIPPV GHLRFPLFVK PISGRGSAGI DEENIVYDKD KLPQVVRKIT EKIGQAALIE EFIEGKEVTV GIIGYKHPQV LPLLEVGYNN VKTNTYEHKM FDNEIIKCPM EVSKEVEEKI KETALNIYKV LNAKDFARID MILSKDNVPY FLELNTFAGL TMSSSKGEKH VHHGYMGYMA KAAGLTRGEF IGKIIESAIE RYKLK //