ID A0A143BJN6_9BACT Unreviewed; 405 AA.
AC A0A143BJN6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=GEMMAAP_08165 {ECO:0000313|EMBL:AMW04813.1};
OS Gemmatimonas phototrophica.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW04813.1, ECO:0000313|Proteomes:UP000076404};
RN [1] {ECO:0000313|EMBL:AMW04813.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW04813.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT "Functional type 2 photosynthetic reaction centers found in the rare
RT bacterial phylum Gemmatimonadetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN [2] {ECO:0000313|EMBL:AMW04813.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW04813.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT bacteria in diverse environments.";
RL Environ. Microbiol. Rep. 8:139-149(2016).
CC -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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DR EMBL; CP011454; AMW04813.1; -; Genomic_DNA.
DR RefSeq; WP_026850585.1; NZ_CP011454.1.
DR AlphaFoldDB; A0A143BJN6; -.
DR STRING; 1379270.GEMMAAP_08165; -.
DR GeneID; 78444113; -.
DR KEGG; gph:GEMMAAP_08165; -.
DR eggNOG; COG0458; Bacteria.
DR OrthoDB; 2210549at2; -.
DR Proteomes; UP000076404; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
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; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF02222; ATP-grasp; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000076404}.
FT DOMAIN 118..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 405 AA; 44450 MW; 8E78ABCD91DF1994 CRC64;
MLVIFVAPFF SPAATQMIEA ALALPHIRLA VIAQQALEQL PPHLAARLVG HWRVNDVTDA
GQLTWAVKGL SAAHGAVSRC FAAYEQTQWP LATVREQLGI PGLPSEAAQN FRDKARMKDV
LRAAGVPVAR HQLVEHAPDA RRFVADVGFP IVIKPPAGAG AKATERITDA SSLEAALQRY
APSPQDPMLA EEFLRGTEHS LETVTINGAP VWHSLTRYAP TPLDVIENPW IQWTVLLPRD
IDTPQYDDIK AMGDKALKVL GMTTGVSHCE WFRRPDGSVA ISEIAARPPG ANITTMVSRA
NDMDFVTAWM RLMIDGRFTV PERRYAVGTA YLRGQGQGIV AAVEGLDLVR RELHHLICDE
RLPYPGQAPT GSYEGEGFIM VRHPDTRVVQ NALTRIISTV KVILR
//
