ID   A0LG59_SYNFM            Unreviewed;       357 AA.
AC   A0LG59;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:ABK16411.1};
GN   OrderedLocusNames=Sfum_0713 {ECO:0000313|EMBL:ABK16411.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16411.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16411.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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; CP000478; ABK16411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LG59; -.
DR   STRING; 335543.Sfum_0713; -.
DR   KEGG; sfu:Sfum_0713; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_0_7; -.
DR   InParanoid; A0LG59; -.
DR   Proteomes; UP000001784; 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; 3.30.1490.20; 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:ABK16411.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN          135..352
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   357 AA;  38952 MW;  230E18FAD35E69BE CRC64;
     MSRARPGTPV VAPSAVHDRF PKCLFMMNTI VLHGLVPEGA AQDEADVLVQ AGAVSTALAA
     LGHLPRLLAL NMDLQAAIDE LLGIRPRLVF NLVESINGSG RFIHFAPSIL EHLRIPFTGA
     RADAILSTSN KLLAKRLLDR AGIRTPPWFE KPGGARRHPG SPFPAGTCLV KSVWEHASIG
     IDENSLVQAR DAGDLMEPIL QREAMLGGEW FAESFIEGRE FNISLIEEAG RVRVLPPAEI
     LFRGFPSDTP KIVGYRAKWE TGSFEFRNTP RTFEFAAEDE GLLRRLSEIS MNCWELFGLN
     GYARVDFRVD GVEVPWVLEV NANPCLSPDA GFIAAAARAG LSYTDVIDRI ASGARCG
//