ID D5ECQ2_AMICL Unreviewed; 350 AA.
AC D5ECQ2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ADE56334.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:ADE56334.1};
GN OrderedLocusNames=Amico_0187 {ECO:0000313|EMBL:ADE56334.1};
OS Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminobacterium.
OX NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56334.1, ECO:0000313|Proteomes:UP000002366};
RN [1] {ECO:0000313|EMBL:ADE56334.1, ECO:0000313|Proteomes:UP000002366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX PubMed=21304712;
RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT 1).";
RL Stand. Genomic Sci. 2:280-289(2010).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP001997; ADE56334.1; -; Genomic_DNA.
DR RefSeq; WP_013047600.1; NC_014011.1.
DR AlphaFoldDB; D5ECQ2; -.
DR STRING; 572547.Amico_0187; -.
DR KEGG; aco:Amico_0187; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_0; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000002366; 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:0000313|EMBL:ADE56334.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000002366}.
FT DOMAIN 127..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 350 AA; 39749 MW; 0FA9C23765FAA526 CRC64;
MTSKEQPTEP PGSGQRPVLI AAAKEYTHRQ DLLDCLICRE DVGCVLSSQG YSIYNLDIFP
ADLADPKHLV QRINEYQPLC VFNLFEGFGS EPWLEASFCE ILEKNNLTFT GNPSGALRLC
IDKHTLHQQL KTAGIPVPLS YFLKGKETLG TLENISFPLF IKPCREDGSV GIDKKSLVFN
EEELQESVTE KLAKFPDGIL IQEFLSGPEY CVSFVDNGPF SPVGLWTLDY SRYPECPAYL
SYDAKWNENS PEWNLWPEEI DLDYSLKETI LHMASRAALV AGCKGYFRVD LRENQGHLFV
MDINPNPALT RDSGMARQYM QKGKTYEQLV MKILQLAILN YKKRDDHENN
//
