ID B8DR84_DESVM Unreviewed; 651 AA.
AC B8DR84;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN OrderedLocusNames=DvMF_2783 {ECO:0000313|EMBL:ACL09721.1};
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL09721.1};
RN [1] {ECO:0000313|EMBL:ACL09721.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL09721.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001197; ACL09721.1; -; Genomic_DNA.
DR AlphaFoldDB; B8DR84; -.
DR STRING; 883.DvMF_2783; -.
DR KEGG; dvm:DvMF_2783; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_7; -.
DR OrthoDB; 9801302at2; -.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro.
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:ACL09721.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 37..89
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 97..480
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 541..625
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 651 AA; 72515 MW; 339788F98DD13110 CRC64;
MPFTGGTIDA LLREERVFRP LPQVVAGAVV NPQDVARARA RAAADPDGYW EEAAEELEWF
RRWDAVHDGS NAPFHRWFTG ARCNIVHNAL DRHIETGTKN RLALIWEGES GDTRSFTYYQ
LYREVNRLAN ALRGLGVGKG DRVIIYMPPL PETVFAMLAA AKIGAVHSTV FGGFSARSLR
DRMEDARPAV IVTVDGFYRN GRVIPLKPIA DEAVATLPPD LAAGVRHMVV VHRAHVETPM
TEGRDIWYHD AVRGQHHEAL TEIMDSTDPL FLLYTSGTTG KPKGHVHAHG GYMVGVHRTM
RWVFDVKPTD IFWCTAEPGW ITGHSYVVYG PLMAGTTTVL YEGHPLYPEP GRVWSMVERL
GITILYTAPT LVRMLMRHGA QHVARHDLTT LRLLGTVGEP ISPEAWLWFH RHVGRGRCPV
LDTWWQTETG MIMLSPLPVS LLKPGSVTRP LPGIEADVVD EHGKPVGPGH GGLLVLQRPW
PAMSCGVYND DESYRRLYWE RFPGWYCTGD VARRDEDGYF WIQGRADDVL LIAGHRIGTA
EMEAALASHR SVAECAVIGV PDALRGEVAK AFVVLVDDHP PLGTMVNADE LAAELVEHVR
RELGPVAVIR EVSFREGLPR NRSGKIMRRV LRSEELGRDT GDLSTLEDGY V
//
