ID A0A133VSH6_9EURY Unreviewed; 894 AA.
AC A0A133VSH6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=AKJ35_00895 {ECO:0000313|EMBL:KXB09383.1};
OS candidate division MSBL1 archaeon SCGC-AAA833F18.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698257 {ECO:0000313|EMBL:KXB09383.1, ECO:0000313|Proteomes:UP000070399};
RN [1] {ECO:0000313|EMBL:KXB09383.1, ECO:0000313|Proteomes:UP000070399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA833F18 {ECO:0000313|EMBL:KXB09383.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456216; EC=6.2.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001619};
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:KXB09383.1}.
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DR EMBL; LHYO01000006; KXB09383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VSH6; -.
DR PATRIC; fig|1698257.3.peg.253; -.
DR Proteomes; UP000070399; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000070399}.
FT DOMAIN 501..537
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 742..894
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 894 AA; 99703 MW; B4DA2FDA0B8B907A CRC64;
MTTRDLDKIF NPDSVAVIGA TDRKGALGRG LTANLIKTYE GEAYPVNPNR DKVFGIRTFS
SVKEIPNSVA LAVIATPAPT VPQIIRECGE VSIPASIIVS AGFRESSPQG EKLEEKIGKI
REEYGMRILG PNSLGVMRPS RNLNATISDK ISSPGGIAFI SQSGALGPSI LDWQAGYEIG
FSSFVSVGNM LDVDFGDLID YFGKDPETRT ILMHVESIRN PKKFMSAAKG FAKTKPIILE
KPGKYPESSK AISSHIGSLP GDDSLYESLF RRSGVVRVEE ISDLFSCSEA LAYKCLPRGP
NLAIITNAGG PGAMATDALL NHEGKLASLS NRTIKKLEKD LAPYTSKSNP IDVSSDANVE
DYLNCIGTCL KDEGVDGILI IYAPQGESYP NQLAKALVKI SEKSEKPILT CWMGREKVQE
SRNVLRNGGI PTLNTPEQGV RIFMYMYEYL RNKKLLYETP KPLSADNIPL KHQDSQRKYL
KTITKRLISE NRSVLTEDES KRFLQTYNIP TIGAYVAHTP EKAADLAEKI GFPVALKIRS
PNIDRESSTG IAASNLESKT EVKEAFKKIV SRAESQYPEA KVRKVIVRKG IRDVHYELSL
GSKKDPRFGS VIFFGRGGID EKLYHNVAVD FPPLNEVHAR RLVERTKVPE LLEELDDEPS
VRLRSLLEYL ARFSQLVIDF PEIKEMELDL AGTKRGLFTV DAQITLDKEG FSVEADPHAH
LIIEPYPLKY IQKKKLKDGR EVTIRPIKPE DEVSVLKFFD TFSEETRRRR FFVPMKEVTH
EDMIRFTNID YWREMAIVGA LEEEEKIIGL GELITEPGED SGEIAVVMGD PWQGLGLGTK
LVESLIEIGK DKHLKKIWGS LQKDNFRMLH ICEKLGFQVE AEYPDMIKVV LTVR
//