ID A0A1F3NZ69_9BACT Unreviewed; 725 AA.
AC A0A1F3NZ69;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A3G23_13420 {ECO:0000313|EMBL:OFY70799.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY70799.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY70799.1, ECO:0000313|Proteomes:UP000176497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY70799.1}.
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DR EMBL; MEPC01000021; OFY70799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3NZ69; -.
DR STRING; 1797365.A3G23_13420; -.
DR Proteomes; UP000176497; 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; 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 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 511..547
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 725 AA; 78995 MW; 8ED0AA65AE05E96B CRC64;
MIFSLEISEK NTYQSLLPLF CPKSIAVVGA SRNPKSIGYR LLEAIVTNKF NGTVYPVNPS
AKFIYSIRAY PEIAVCPEKI DLAIISVPAL IVPQAIDNCI KADVKAIILI SAGFAETGKE
GKVLQNEILN RVREKGIRMV GPNCMGMLNA SPDISMNASF SITLPPFGNV AMSSQSGALG
LAVITHAKKL NIGLSSFVSV GNKADISAND LLHYWENDSD TKVILLYIES FGNPRKFVKL
ARRIGKNKPV LAVKSGRTKS GIRAAGSHTA SLASNEIAVE ALFNQTGVIR ANTLEEMFDI
TAILSNQPLP LNNKVGVITN AGGLAILCAD ACESENLVLP EFSETIKSKL RTFLPAEAAI
SNPVDMVASA TPESYYKAIK TIMASDEIDS LIILHIPVDD SDSDKFFNSI NSAVSETRNT
PEGKNKPVVG CLMYDENFLK SILSSSKMPL YRFPESAGRS LAKVVKYSAW KNKPLGVLRD
FKDTHIENAR KICLNALHER GKGWLKAKEI HELFSAFSIS LPESGITTNE FSAAEIARKM
GFPVVLKLSS HTIIHKTEVG GVYLNLNNEQ EVIEAFLHLK QKMALLNKSD EMDGVLIQKM
LMDPVEVMIG MVEDNTFGPI VAFGMGGIHV EVISDICFRI TPLNDLDAKE MIRSIKGFKL
LSGYRGHPAA DIPALEELLL RISKLVEEIP EIKELDLNPV FALAPGKGCV IGDARIFVSD
KLSIT
//
