ID A0A0S8DQ40_9GAMM Unreviewed; 414 AA.
AC A0A0S8DQ40;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=AMJ69_09900 {ECO:0000313|EMBL:KPK37910.1};
OS Gammaproteobacteria bacterium SG8_47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703406 {ECO:0000313|EMBL:KPK37910.1, ECO:0000313|Proteomes:UP000054199};
RN [1] {ECO:0000313|EMBL:KPK37910.1, ECO:0000313|Proteomes:UP000054199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_47 {ECO:0000313|EMBL:KPK37910.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK37910.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTV01000103; KPK37910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DQ40; -.
DR STRING; 1703406.AMJ69_09900; -.
DR PATRIC; fig|1703406.3.peg.380; -.
DR Proteomes; UP000054199; Unassembled WGS sequence.
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 Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR041472; BL00235/CARNS1_N.
DR InterPro; IPR040570; LAL_C2.
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 Pfam; PF18130; ATPgrasp_N; 1.
DR Pfam; PF18603; LAL_C2; 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 112..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 414 AA; 44467 MW; D5736AF10B147595 CRC64;
MTDRVLIIAP HGSYRTFPFI EAAEKMGVEV LIASEGKHSI VSAYAHGLHI DCTDQDQALR
SILAEAAQHG FVGIVGTDDA STELAAMAAK ALNLPHNDPL AVAIARRKDR ARECLHQAGV
RVPEFRQVAL SEVADAAAQV GYPCVIKPLA LSASRGVIRV DNMSELDQAC RRIAAILHAA
EGLVDEERSH VLVERFVPGT EVAVEGMLNA GSLQILALFD KPDPLDGPYF EETYYVTPSR
HSAAEQADIE HCVAQACAAY GLREGPVHAE CRLNEQGVWL IEMAARTIGG LCARLLRFGT
GYQLEELVLA QACGKPIKPE TIAEAAGVLM LPIPRAGVLR RVEGLLAAQR VPYVEEVTIL
VREGHQLVPL PEGSSYLGFV FARASSPALV EAALREAHAA LNVVVAPLWE AQVA
//