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Database: UniProt
Entry: A0A133VSH6_9EURY
LinkDB: A0A133VSH6_9EURY
Original site: A0A133VSH6_9EURY 
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
//
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