ID A0A0S8GSR7_9BACT Unreviewed; 651 AA.
AC A0A0S8GSR7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=AMJ79_13510 {ECO:0000313|EMBL:KPK74666.1};
OS Phycisphaerae bacterium SM23_30.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK74666.1, ECO:0000313|Proteomes:UP000051901};
RN [1] {ECO:0000313|EMBL:KPK74666.1, ECO:0000313|Proteomes:UP000051901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_30 {ECO:0000313|EMBL:KPK74666.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK74666.1}.
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DR EMBL; LJUC01000204; KPK74666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8GSR7; -.
DR STRING; 1703411.AMJ79_13510; -.
DR PATRIC; fig|1703411.3.peg.1854; -.
DR Proteomes; UP000051901; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KPK74666.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 29..85
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 92..474
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 536..614
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 651 AA; 73021 MW; 7F62EA592EC15056 CRC64;
MAVEQTSTVP LYDVPETIKG KTDIDWEKYQ QMYRWSVEDA EGFWAAMAEK FLTWQRRWDE
VLNWDFKTAR VEWFKGGKLN VCYNCLDRHV EAGHGGQTAL IWEGNEPTED ARFSYQDLLE
QVCRFANALK GLGVKKGDRV CLYLQMIPEL PMAMLACARI GAVHNVVFGA FSPDSLAERI
NDSSCKVLVT QDAALRGEKK NIPMKTKADE AVKICPSIEH TIVIRRTGLE VPMTEGRDLW
WHEVTKQEPT DCQWVLMDAE DPLFILYTSG STGHPKGVVH STGGYLLYAA ITQKYLFDYQ
PGDVHWCTAD IGWVTGHSFV VYGPLCNQAL TVVFEGVPHY PDFGRFWQII AKYKVTNFFT
APTALRSLMK EGDGWVEKHD LSSLKVLLSA GEPIKSREWH WYYQVVGKKR CPVVDNFWQT
ETGSALLTPL PGATKTKPGS ATFPFFGIRP EIMDETGAVL QGPNVSGDLC IAFPWPGMAR
TVYGDHDRFV ENYFSLYPGK YFTGDGCRRD EDGYYWITGR VDDVINVSGH RLGTAELEGA
LGKHPAVAEA AVAGFDHEIK GNGIYAYVTL KTGQQPSEAL KKELIQTVRR EIGPHASPDK
IQFTPGLPKT NSNKIIRRIL RKISEGDIDD LGDLTTLANP KVVEDLIAGR L
//
