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Database: UniProt
Entry: L0FCJ7_DESDL
LinkDB: L0FCJ7_DESDL
Original site: L0FCJ7_DESDL 
ID   L0FCJ7_DESDL            Unreviewed;       416 AA.
AC   L0FCJ7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   05-FEB-2025, entry version 44.
DE   SubName: Full=Phosphoribosylamine-glycine ligase {ECO:0000313|EMBL:AGA70381.1};
GN   OrderedLocusNames=Desdi_2974 {ECO:0000313|EMBL:AGA70381.1};
OS   Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Desulfitobacteriaceae; Desulfitobacterium.
OX   NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA70381.1, ECO:0000313|Proteomes:UP000010797};
RN   [1] {ECO:0000313|Proteomes:UP000010797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
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., Boon N., Smidt H., Woyke T.;
RT   "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003344; AGA70381.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0FCJ7; -.
DR   STRING; 871963.Desdi_2974; -.
DR   KEGG; ddl:Desdi_2974; -.
DR   eggNOG; COG0151; Bacteria.
DR   HOGENOM; CLU_029016_5_0_9; -.
DR   Proteomes; UP000010797; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; IPR052032; ATP-dep_AA_Ligase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR040570; LAL_C2.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF18603; LAL_C2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AGA70381.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000010797}.
FT   DOMAIN          110..303
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   416 AA;  46160 MW;  19ACC3ECA4EF9D33 CRC64;
     MTLARLLILG GSNIQINAIL RAKEKGHMVI VADYLDDAPG KKFADYSELT STFDAQGCLA
     VARKYKIDGI LTVGTDQPVL TCAKVANELG LPSFLDSEQA QAVTHKKVMK KIFKENEIPS
     AEYRLIQKDF EEAELGAIRF PAVMKPLDSQ GQRGVYKVES LQQIRSLLPD VLSYSREDEI
     LIEEFYPSEE ITLSGWVRDR KAHILTVTDR QTIANGQHIG ICIAHHFPSK YLAEYAKEIE
     ELTDKIVQAF DIQCGPIYFQ MLIGSEGIKV NEIACRIGGA YEDELLPVIT GVDILEMLIL
     HASGQDVDYT ALEHYELKNN TNHASVQMIF TKPGTIGRMA PMEGIVVRSG AITGGFNYDV
     GSTIQEIQNA TQRVGYMLFQ GDSATGLKTK IEKALACLEI RDIQGKNMLV DLHCQK
//
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