ID A0A099D5H2_9ACTN Unreviewed; 427 AA.
AC A0A099D5H2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoribosylglycinamide synthetase {ECO:0000313|EMBL:ASU78659.1};
GN ORFNames=CDG81_10660 {ECO:0000313|EMBL:ASU78659.1}, IL38_10690
GN {ECO:0000313|EMBL:KGI81418.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU78659.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:KGI81418.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI81418.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU78659.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU78659.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022752; ASU78659.1; -; Genomic_DNA.
DR EMBL; JPMV01000018; KGI81418.1; -; Genomic_DNA.
DR RefSeq; WP_043573035.1; NZ_KN214176.1.
DR AlphaFoldDB; A0A099D5H2; -.
DR KEGG; aey:CDG81_10660; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_029016_3_1_11; -.
DR OrthoDB; 24041at2; -.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR SMART; SM01209; GARS_A; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 116..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 427 AA; 46904 MW; 82B451FD820CDDCA CRC64;
MSDTSGRAVA VVVDGYSAGN FYPPAFAELG VDLVHVQSTP ELIPAMAPPQ LSRYRENILG
ADEREWARRL RPYEPVCVVA GQESAVEPTD RLAEELRLPG NGTRLSTARR DKYEMVETLR
RSGVRCARQF KSDSPRALAR WAEHNDDYPV VVKPLSSAAS DGVTICFDAD EVATAAESVL
ASQNIFGTAN TEILVQSYLA GTEYIVDTVS CDGHHYVCGV WEYEKTLLPS GDNIYNRDIL
ADPSREPVPA LIDYAHEVLD ALDVRWGPAH AEIIMTEQGP ALVEIGTRLN GNLDAGFHDV
CLGHNQAALS ALAYVSPETF LRRYTDRVYT KHQPAFVYNT PTELDGTVES VDQEVVDEIR
GLESVHHAAV KVAAGGRIRP TTDLLTSSMR VFLTAPEESR LEADYEKVRS LKDSVYQLAE
QHADGSA
//
