ID I7KZD9_METBM Unreviewed; 632 AA.
AC I7KZD9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN OrderedLocusNames=BN140_1312 {ECO:0000313|EMBL:CCJ36235.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ36235.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
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DR EMBL; HE964772; CCJ36235.1; -; Genomic_DNA.
DR RefSeq; WP_014867211.1; NC_018227.2.
DR AlphaFoldDB; I7KZD9; -.
DR STRING; 1201294.BN140_1312; -.
DR GeneID; 13355375; -.
DR KEGG; mbg:BN140_1312; -.
DR PATRIC; fig|1201294.9.peg.1446; -.
DR HOGENOM; CLU_000022_3_6_2; -.
DR BioCyc; MBOU1201294:BN140_RS06545-MONOMER; -.
DR Proteomes; UP000009007; Chromosome.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCJ36235.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007}.
FT DOMAIN 30..83
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 86..477
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 531..609
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 632 AA; 71283 MW; DEF22FE86FAEF6B6 CRC64;
MTENFSVKLE EAKYYTPEVR CREQSWMGNY NKTYQAFLAD PDGFWDNVAR ELEWFQPWSR
VKEWDYPYAR WFLNGKLNIT HNCLDRHAHN QRRNKVALMW RGETEDEERI YTYRQLFQAV
CRFANGLKSL GVGKGDRVCI YMPVVPEQVI AMLACARIGA VHSVVFGGFG VNALNQRIRG
TNAKVVITAD VTYRRGRAIP LKNIVEEAVV NAPSVERIVV LRRDTDKPVE LHPEMEVDYY
DLVDGESREC PAEPMDAEDP LFILYTSGTT GAPKGIVHAC GGYTVGTYYT TKHVFDIRDD
DIYWCTADPG WITGHSYGIY GPLLNGATCL IAEATPDYPT PGTWWDLIEE YGVTIFYTAP
TAIRMFMRVG EEWPNRYNLS SLRILGSVGE PLNPEAFEWF YHTIGKDRCP IVDTWWQTET
GMHMLTTMIG EPMRPGFVGR PIPGVVADVV NRQGKPVPPG TGGLLVIKEP WPSMMRTVWG
DDERYRKYWE TIPGCYTAAD LAVKDEDGYI MVIGRADDLI VVAGHNIGTA EVESALVSHD
AVAEAAVIGK PDPLKGNTIK AFVILRDGQQ PGEKLKKDLI YHVRMTLGPI AIPSEIDFVQ
SLPKTRSGKI MRRVLKAQEM GMDPGDISTL EE
//
