ID A0A0A7KB43_9FLAO Unreviewed; 635 AA.
AC A0A0A7KB43;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=M666_12955 {ECO:0000313|EMBL:AIZ42409.1};
OS Cellulophaga baltica 18.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=1348584 {ECO:0000313|EMBL:AIZ42409.1, ECO:0000313|Proteomes:UP000030786};
RN [1] {ECO:0000313|EMBL:AIZ42409.1, ECO:0000313|Proteomes:UP000030786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18 {ECO:0000313|EMBL:AIZ42409.1,
RC ECO:0000313|Proteomes:UP000030786};
RX PubMed=24428166; DOI=10.1111/1462-2920.12391;
RA Holmfeldt K., Howard-Varona C., Solonenko N., Sullivan M.B.;
RT "Contrasting genomic patterns and infection strategies of two co-existing
RT Bacteroidetes podovirus genera.";
RL Environ. Microbiol. 16:2501-2513(2014).
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DR EMBL; CP009976; AIZ42409.1; -; Genomic_DNA.
DR RefSeq; WP_029446200.1; NZ_CP009976.1.
DR AlphaFoldDB; A0A0A7KB43; -.
DR STRING; 1348584.M666_12955; -.
DR GeneID; 78061648; -.
DR KEGG; cbat:M666_12955; -.
DR HOGENOM; CLU_000022_3_6_10; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000030786; Chromosome.
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:AIZ42409.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 12..68
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 70..462
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 519..598
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 635 AA; 71796 MW; 0DF65BB597AC351B CRC64;
MSNYHIKHLE EYFQVYRKSV RNPEAFWEEI AEEHFLWRKK WDKVLSWDFS KPEVTWFEGA
QLNITENCID RHLATRGEKT AIIFEPNNPE EEAQHISYYQ LHDKVCRMAN VLKEKGIKKG
DRVCVYLPMI PELAVTILAC ARIGAIHSVV FAGFSSNALA TRINDSDCKI VITSDGSYRG
NKSIDLKGIV DKALEECPGV AHVLVAKRTK STIEMKNGRD EWLQPLLDAA YGDCVPEIMD
AEDPLFILYT SGSTGRPKGM VHTTGGYMVY TAYTFKNVFQ YRENDVYWCT ADIGWITGHS
YIVYGPLANG ATTVMFEGVP SYPDFGRFWD VIEKHKVNQF YTAPTAIRAL AKQNLEFVEN
HDLSSLKVLG SVGEPINEEA WHWYNNNVGK KKSPIVDTWW QTETGGIMIT PIPYVTPTTP
TYATLPFIGI QPALMDEEGH EIMGNQVEGR LCIKFPWPSM ARTIWGDHDR YRDTYFTAYK
NNYFTGDGAL RDAVGYYRIT GRVDDVIIVS GHNLGTAPIE DAINEHPAVA ESAIVGFPHD
VKGNALYGYV ILKETGETRD RDNLRNEINQ QITEHIGPIA KLDKIQFVSG LPKTRSGKIM
RRILRKIASN DVSNLGDTST LLNPEVVQEI IDNVV
//
