ID A0A1Q7MC97_9CHLR Unreviewed; 621 AA.
AC A0A1Q7MC97;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:OLD10296.1};
GN ORFNames=AUJ06_02355 {ECO:0000313|EMBL:OLD10296.1};
OS Chloroflexi bacterium 13_1_40CM_3_70_6.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805073 {ECO:0000313|EMBL:OLD10296.1, ECO:0000313|Proteomes:UP000187353};
RN [1] {ECO:0000313|EMBL:OLD10296.1, ECO:0000313|Proteomes:UP000187353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD10296.1}.
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DR EMBL; MNGP01000039; OLD10296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7MC97; -.
DR Proteomes; UP000187353; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF232; ACETYL-COENZYME A SYNTHETASE; 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.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 128..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..63
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 67..403
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 498..576
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 621 AA; 68373 MW; 9F0BCFE59A66B695 CRC64;
MSPADARRRV MDWKREAASD PEGFWGRAAE QVPWFKKWER VLDWEPPTFR WYRGGLSNLA
YNAVDHHVAA GQGDRIALIT ENERGERRKL TYAELHRETK RVGAALRGMG ITKGDRVAIY
MPTCAEAIIL MLGAVRIGAV ILVVFAGFGA GALGERIRLA GARVLFATDV TYRKGKDVPL
LPIVAQAVAY APTVERVVLL RRAASGDRVR NEISWGEFLA GAEGHDDSHV ELEANEPAYI
LATSGTTAKP KLAVHTHGGY QVYVYSMAKW MFGLRENDVW WSTSDIGWVV GHSYIVFGPL
LVGCTTIAYE GALDHPNAET FYAIVERNAV TGVFTSPTAA RLLGRYGTAP AWKHDLSSLE
RLFCAGEVLN APAWEWLQKE ALRDRVPVID HYWQTETGGP VVGNPYGVAL LPIKPGSGGV
LPAGEKGIFV IKRPFPGLTA RLWAEPERYA GDYWERVPGK TVYFTGDASS IDEDGYVWFS
GRADEIIKIA DHRLGTIEVE TAFLRHPAVA EAGVTGRPDE LRGQVISAFV VLKQGSVPSD
QLRRELLDTV RNELGPVAVI GELNFVDMLP KTRSGKIMRR VLKAVILDKD PGDISTIEDE
GSVEEAREAW DQMKTSVAAG D
//
