ID A0A1A7BIV6_9SPHN Unreviewed; 335 AA.
AC A0A1A7BIV6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphoribosylglycinamide synthetase {ECO:0000313|EMBL:OBV12488.1};
GN ORFNames=I603_0619 {ECO:0000313|EMBL:OBV12488.1};
OS Erythrobacter dokdonensis DSW-74.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1300349 {ECO:0000313|EMBL:OBV12488.1, ECO:0000313|Proteomes:UP000092484};
RN [1] {ECO:0000313|EMBL:OBV12488.1, ECO:0000313|Proteomes:UP000092484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSW-74 {ECO:0000313|EMBL:OBV12488.1,
RC ECO:0000313|Proteomes:UP000092484};
RA Kim J.F., Song J.Y.;
RT "Genome sequence of Porphyrobacter dokdonensis DSW-74.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBV12488.1}.
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DR EMBL; LZYB01000001; OBV12488.1; -; Genomic_DNA.
DR RefSeq; WP_068862303.1; NZ_LZYB01000001.1.
DR AlphaFoldDB; A0A1A7BIV6; -.
DR STRING; 1300349.I603_0619; -.
DR PATRIC; fig|1300349.4.peg.616; -.
DR Proteomes; UP000092484; Unassembled WGS sequence.
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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 121..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 335 AA; 37566 MW; CA4B610880852AFB CRC64;
MSSYPSPLRI PEDAKQRLKI MFIAKNALWD GTGSAEDGNH ATYHVEMREV LKGLGLNLRV
ENRFEVLFDK PDVDFVFPLL NRAGFFNSEM LCPLLCERAG IPYLGASPIL RGLSDDKHLA
KRAVRDAGVP TAPWAIYRRG APIDPAKCPA GSRFVVKPNN SSASWGVMDA TDWASVEKAI
HGVHELGHDA LVEPFIDGSD VEVPVVTING EPVILPMMIF RQADPSHLRT YQEKRDLVDR
SQKYSLDPFE NPEMIAKITE YTKAAMQEYR PFDYGRWEFR VNEETGDITF LELNLNCNLW
SQKVFGRAAA LAGWSHPELI ETLLAESLSR HGLLG
//