ID A0A1F8NZC8_9CHLR Unreviewed; 699 AA.
AC A0A1F8NZC8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A2Y93_09130 {ECO:0000313|EMBL:OGO16253.1};
OS Chloroflexi bacterium RBG_13_68_17.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797638 {ECO:0000313|EMBL:OGO16253.1, ECO:0000313|Proteomes:UP000178211};
RN [1] {ECO:0000313|EMBL:OGO16253.1, ECO:0000313|Proteomes:UP000178211}
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:OGO16253.1}.
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DR EMBL; MGNF01000014; OGO16253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8NZC8; -.
DR Proteomes; UP000178211; 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 490..526
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 699 AA; 72952 MW; 7E2990F1AEA65031 CRC64;
MLESFFSPRG VAVVGASQNP GKLGYGVARN LVLSGYAGAI HFVNPHGGRL FERPIYADLA
SVPDPVDLAM ILIPGAAVPE ALQACGRRGI KAVIIGSGGF RETGPEGQAL EERCREVARR
EGIRVLGPNC IGLLDTHLPI DTTFLPLPGP IPGDIAFLSH SGAICEAVID WARGQGFGLS
RLVSLGNQMD LTEGEVIGPT AADPHTRVVA MYLEGVGDGA AFVEQVRRVT RIKPVIAIKV
GRSRGGREAV ASHTGALAGQ DAAYEAAFRK AGVIRADTTE EVFDWARALA WCPLPGGRRV
AVLTNAGGPG AIAADALEAN GLEQARLSDT TQQQLRQLLP PAASLRNPID MLAGAGPSEY
AAALGMLLAD EGVDAAMVIL VPPPMTTAAE VAGAVIPLIR SAEKPVVMVL MGEDLITHAA
RLLRQARIPD YRFPERAASA LRVLADRARR LQEPEEEPMV VAGIESGAAG SILAAARTGA
NGFVDPQTAA AVIASYGIAV PPATVAQSEA EAAEAAARIG WPVVAKLISP DRSHKSDIGG
VVVGLRSRDE VRQAYRQIVA GAQEVGAAVG GVLVQSMANE GQEVIIGVVR DEQFGPLVMF
GSGGVEVEGL RDVAFALAPL TAADGRALLD STWAGRRLAG FRSLAAGDRE AVVDALTRLG
RLVTDYPQVI EIEINPLRVL PPGKGALALD VRLRLADRS
//
