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Database: UniProt
Entry: A0A0F7GD07_9CHLR
LinkDB: A0A0F7GD07_9CHLR
Original site: A0A0F7GD07_9CHLR 
ID   A0A0F7GD07_9CHLR        Unreviewed;       314 AA.
AC   A0A0F7GD07;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Dalaninedalanine ligase {ECO:0000313|EMBL:AKG53356.1};
GN   ORFNames=DGWBC_0680 {ECO:0000313|EMBL:AKG53356.1};
OS   Dehalogenimonas sp. WBC-2.
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX   NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG53356.1, ECO:0000313|Proteomes:UP000034106};
RN   [1] {ECO:0000313|EMBL:AKG53356.1, ECO:0000313|Proteomes:UP000034106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WBC-2 {ECO:0000313|EMBL:AKG53356.1,
RC   ECO:0000313|Proteomes:UP000034106};
RX   PubMed=26452554; DOI=10.1128/AEM.02017-15;
RA   Molenda O., Quaile A.T., Edwards E.A.;
RT   "Dehalogenimonas sp. Strain WBC-2 Genome and Identification of Its trans-
RT   Dichloroethene Reductive Dehalogenase, TdrA.";
RL   Appl. Environ. Microbiol. 82:40-50(2015).
RN   [2] {ECO:0000313|Proteomes:UP000034106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106};
RA   Molenda O., Edwards E.A.;
RT   "Identification of trans-1,2-dichloroethene reductive dehalogenase (TdrA)
RT   in Dehalogenimonas sp. WBC-2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP011392; AKG53356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7GD07; -.
DR   STRING; 943347.DGWBC_0680; -.
DR   KEGG; dew:DGWBC_0680; -.
DR   Proteomes; UP000034106; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
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   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:AKG53356.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          99..309
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   314 AA;  34163 MW;  C7D19CDBA6A7B32D CRC64;
     MLGESEAENG VLDAVKAVRR AIRALGYDYV ELPLNLPIES VYETLSKLRV NIVFNLFEGF
     AGMPATEAVI AGFVEKLGLP FTGSSSQTLT LALDKAAANQ RLRSNGVRTA NQQLLTARDL
     DRFHLGFPCI VKPRADDASH SLSEKSVVFD MDALSREVDA MVNRYDGTAA LVEEFLEGRE
     FNATVWGVDS PVVLPLSEII YTLPEGLPKI LTFAAKWEPK SMYFAHTAVQ CPANVTPDLR
     AAIQSTALMA FKAIGCQGYG RVDMRLNKDG HPVVMEVNAN PDIAPGTGVA RQVKAARLSY
     KAMVSKIIDF GLVK
//
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