ID A0A135VI56_9ARCH Unreviewed; 696 AA.
AC A0A135VI56;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:KXH72350.1};
GN ORFNames=AM324_07560 {ECO:0000313|EMBL:KXH72350.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-83.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH72350.1, ECO:0000313|Proteomes:UP000070043};
RN [1] {ECO:0000313|EMBL:KXH72350.1, ECO:0000313|Proteomes:UP000070043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH72350.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(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:KXH72350.1}.
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DR EMBL; LRSK01000210; KXH72350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VI56; -.
DR Proteomes; UP000070043; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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 696 AA; 75228 MW; 2C8A68C3E7720BB4 CRC64;
MDVLFNPRSI AVVGASATEG KLGNDVVKNL LESEFEGRIY PVNPRGGEIL GLKTYRRVSE
IGGRLDVAVI VIPAKYVLSV VEECGNKGVK ALVVITAGFK EMGHEGQEAE KELIAIAEKH
GMIVLGPNCL GIINTHSPYN ASFAAGTPEK GTIAFASQSG ALMTGILDWS LMEKIGFSKF
VSLGNKAQLD EADFVEAFGR DPNTTFILLY IESVMNGRKF MEACRKVTPN KPVFVVKGGV
SAAGARAASS HTGSLAGSDT AYSVAFRQCG VMRADSMAEL FDVANVFDDC NLPKGNRVAI
VTNAGGPGIL TTDACEENGL QMAQFSQATI EELRKGLPPA ASVYNPVDAL GTAQPEDYAV
SLEAVFNDEN VDSVLVLLTP QAMTKETRTA QILVEARRKY PGKPLLAVFM GGNAMTYPRI
VLNEGGVPVF DFPGRAVNAL AELYRYLVLR DSLREESPPD FKVDKKRVER IIKSVREDDR
QVLLGSEAHE MAEAYGIPVA RIKLATSAQE AKEIAAQLGF PVVLKIASPD IIHKTDIGGI
QVGLDDEEEV ENAFLEILDN VRTHMPRAVI YGVDVQEMAE KGKELIIGCS QDIQFGPLLM
FGAGGIYVNF LKDVSFRLAP MTRKDAAELI TETKMGTLLK GVRGEEPSDI EAIEDTILRI
SKLVTDFEEI VELDINPAFA YERGKGISAV DVKITI
//
