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Database: UniProt
Entry: Q1NKA4_9DELT
LinkDB: Q1NKA4_9DELT
Original site: Q1NKA4_9DELT 
ID   Q1NKA4_9DELT            Unreviewed;       429 AA.
AC   Q1NKA4;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   ORFNames=MldDRAFT_2323 {ECO:0000313|EMBL:EAT02136.1};
OS   delta proteobacterium MLMS-1.
OC   Bacteria; Proteobacteria; Deltaproteobacteria.
OX   NCBI_TaxID=262489 {ECO:0000313|EMBL:EAT02136.1, ECO:0000313|Proteomes:UP000005853};
RN   [1] {ECO:0000313|EMBL:EAT02136.1, ECO:0000313|Proteomes:UP000005853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT02136.1,
RC   ECO:0000313|Proteomes:UP000005853};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of delta proteobacterium
RT   MLMS-1.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAT02136.1, ECO:0000313|Proteomes:UP000005853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT02136.1,
RC   ECO:0000313|Proteomes:UP000005853};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D.,
RA   Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of delta proteobacterium
RT   MLMS-1.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAT02136.1}.
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DR   EMBL; AAQF01000290; EAT02136.1; -; Genomic_DNA.
DR   RefSeq; WP_007294907.1; NZ_AAQF01000290.1.
DR   EnsemblBacteria; EAT02136; EAT02136; MldDRAFT_2323.
DR   PATRIC; fig|262489.9.peg.1104; -.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000005853; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005853};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:EAT02136.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005853}.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   429 AA;  45813 MW;  8C7608919AAE19D6 CRC64;
     MKILLIGGGG REHALAWSFA RSPGVGKIYC APGNAGLASL ATLVDIAPND SRALAEFVQQ
     EGIDLTVVGP EEPLSRGIVD YFQERGLRIF GPSKRAAALE GSKVFMKNLL HRYQIPSAAY
     AVFREREAAV AHLDTVEWPV VIKADGLAAG KGVVVAADRA AAVAAIDLIL GERAFGSAGD
     ELVIEEFLDG EEASFIAFTD GRTVLPLPSS QDHKAAYDGD QGPNTGGMGA YSPAPVLTPE
     LERQVLEQIM YPTVAAMAAE GRPYRGMLYA GLMVKDGRAR VLEFNCRFGD PEAQPLLLRL
     QSDLTEVVEA AIDQRLAEIT LRIDPRPAVC VVMAAGGYPG KYDKGHPIKG LEEAAAREGV
     VIFHAGTQRD QEGLVTAGGR VLGVCGQAAT LEEAIERAYQ AVTLISWPDC RYRRDIGRKA
     LERTASGTS
//
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