ID B0EEF5_ENTDS Unreviewed; 713 AA.
AC B0EEF5;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=EDI_135220 {ECO:0000313|EMBL:EDR27069.1};
OS Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN [1] {ECO:0000313|Proteomes:UP000008076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT "Annotation of Entamoeba dispar SAW760.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS548949; EDR27069.1; -; Genomic_DNA.
DR RefSeq; XP_001736656.1; XM_001736604.1.
DR AlphaFoldDB; B0EEF5; -.
DR EnsemblProtists; EDR27069; EDR27069; EDI_135220.
DR GeneID; 5881693; -.
DR KEGG; edi:EDI_135220; -.
DR VEuPathDB; AmoebaDB:EDI_135220; -.
DR eggNOG; ENOG502QWQW; Eukaryota.
DR OMA; IVIYMES; -.
DR OrthoDB; 474at2759; -.
DR Proteomes; UP000008076; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR014089; AcCoA-synth-alpha.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR02717; AcCoA-syn-alpha; 1.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 489..525
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 713 AA; 77495 MW; 4468D4C7ED076D24 CRC64;
MQFEPLFNPK SVAVIGASDR KESVGYAVMN NMIKGGYKGH LYPVGRKPEL FGMKCYAKIG
QIEEKVDLAV IAIPAKFVPG VCIECGEAGV KGLIIITAGF AEAGEEGKKM CIEIQATCQK
YNMRMIGPNC LGIINPRDGV NASFASVMPE AGGVAFISQS GALCTAILDW AANQHVGFSY
FVSIGSSIDT DYADLFEFFA KDPKVTSILM YIESIKDAKK FVLRAREFAA DKPIILLKAG
KSSEGAAAAM SHTGSLAGND AVYDAVFDRC GCIRVDSICD LWDCAHVLAT QNIPQNNRLC
IITNAGGPGV ISTDRLVSVH GHLAKLSEST MTELNGFLSP FWSHSNPVDV LGDATASTYQ
KTLDVVIKDP QIDGVVVVLT PQAMTDPVAV AKSLVEHGPY QKPVLASWMG QSEVEAGVKI
LEQGKIPNFE TPERAVTAFG YIMRHPDIAA KLKEIPKYLD VQVDYEGAKK LIADVVADGR
TTFTEYEGKM MFSKYGIPIK GMAKASTEDE AVAEAMKIGT PVVMKILSPD IMHKTDVGGV
KVKLTTEEEI RKAYRDIMTS VKEKKPEARI HGVLLEKMVG FKYECIIGCK KDPLFGPVIV
FGMGGVTVEL YKDTNIALPP IGLQEADRLI DGTKISKLLR GYRGMPACDV EGLKKILVQF
SKMIMDFPEI SEVDINPLAV SYEEFLVLDA KIVLDKNMIG KEVPKYSHLV IQP
//