ID L9VNG5_9EURY Unreviewed; 706 AA.
AC L9VNG5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=C496_17757 {ECO:0000313|EMBL:ELY38492.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY38492.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY38492.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY38492.1,
RC ECO:0000313|Proteomes:UP000011599};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY38492.1}.
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DR EMBL; AOHW01000042; ELY38492.1; -; Genomic_DNA.
DR RefSeq; WP_006091630.1; NZ_KB913017.1.
DR AlphaFoldDB; L9VNG5; -.
DR STRING; 1114856.GCA_000383975_00227; -.
DR PATRIC; fig|1114856.3.peg.3682; -.
DR eggNOG; arCOG01340; Archaea.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000011599; 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: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; 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.
PE 4: Predicted;
FT DOMAIN 7..100
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 706 AA; 75461 MW; 4FB10AA981009AEB CRC64;
MGRLSALFDP QSVAVVGATD REGAVGRAIL ENLRDEFDGE VVPIHPTRDE VLGIECYADV
SSAPPIDLAV VVVPPDAVIE TLRDAGEAGT ENVVVITAGF AETGSEGATR ERELRAVADE
YDLNVVGPNS LGIMSTPNGM NATFGPENAL EGSISFMSQS GAFITAVLDW ANEQEIGFQD
VVSLGNKAVL DETDFVREWG EDPETDVIIG YLEGIDDGDE FIDAAREVTD NTPIVLVKSG
RTDAGAQAAS SHTGAIAGSE RAYEAGLEQA GVIRANSVQE LFDYARALSG LPEPDHDGVA
VVTNAGGPGV LTTDAVGDSR LEMATFTDET IAALTERMPE EANVYNPIDA IGDADVERFG
EALDIALGDP NVGSAVVVSA PTAVLQYDKL AETVIEKRED HDTPVVTCLM GGERARAAEE
VLREFGIPNY FDPARAVSGL DALARFRDIR ERTIDDPQRF DVDRERAREI LERATRRDDN
RLGVESMDLL EAYGIPIPAG EIVDDPERAR EIAASIEGDV VMKIVSPDIS HKSDIGGVKV
GVANDDVYDA YEDLVARARN YQPDAAILGV QVQELVDLDT ATETIVGVNR DPQFGPLLLF
GLGGIFVEIL EDTSVRVAPI GADEARAMVD EIQAAPLLRG ARGREPADTE QVVETIQRLS
QLVTDFPSIL ELDVNPLVAG PNGVQAIDLR LTVDTETLET DDTEKA
//