ID I3Z062_AEQSU Unreviewed; 635 AA.
AC I3Z062;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN OrderedLocusNames=Aeqsu_3201 {ECO:0000313|EMBL:AFL82630.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL82630.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL82630.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003280; AFL82630.1; -; Genomic_DNA.
DR RefSeq; WP_014783879.1; NC_018013.1.
DR AlphaFoldDB; I3Z062; -.
DR STRING; 746697.Aeqsu_3201; -.
DR KEGG; asl:Aeqsu_3201; -.
DR PATRIC; fig|746697.3.peg.3251; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_10; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000006049; 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:AFL82630.1};
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 71..463
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; 71843 MW; D518D64C25CDCC71 CRC64;
MSNYHIKNLE EYFQVYRKSV RDPENFWEEI AEENFMWRKR WDKVLEYDLS KPEVSWYKGA
KLNITENCID RHLYARGNKT AIIFEPNNPS EEAEHITYNQ LHDRVCRFAN VLLDHGVKKG
DRVCIYLPMI PELAVSLLAC ARIGAIHSVV FAGFSSTALH TRINDSDCKM VITSDGSYRG
GKTIDLKGIV DEAMNSCPNV KTVLVAKRMN SEITMKEGRD KWLQPLLDEA SNQCAPEIMD
AEDPLFILYT SGSTGKPKGM VHTTAGYMVF TAYTFKNVFQ YRENDVYWCT ADIGWVTGHS
YIVYGPLANG ATTVLFEGVP SYPDFGRFWQ VIEKHKINQF YTAPTAIRAL AKERLDFSAN
YDLSSLKILG SVGEPINEEA WHWYNDNIGK KNCPIVDTWW QTETGGIMIS PIPYSTPTIP
TYATLPLPGI QPALMDENGD ELKGNLVSGR LCIKFPWPGM ARTIWNNHER YRETYFSTFK
NNYFSGDGAL RDSTGYYRIT GRVDDVIIVS GHNLGTAPIE DAINEHPAVA ESAIVGFPHD
VKGNALYGFV ILKETGETRL HENLRKEINQ IITEHIGPIA KLDKIQFTTG LPKTRSGKIM
RRILRKIAEK DTNNLGDIST LLNPEVVQEI MDGAI
//
