ID A0A1I0W3N4_9CELL Unreviewed; 917 AA.
AC A0A1I0W3N4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SFA82506.1};
GN ORFNames=SAMN05421867_102114 {ECO:0000313|EMBL:SFA82506.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFA82506.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFA82506.1, ECO:0000313|Proteomes:UP000199012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFA82506.1,
RC ECO:0000313|Proteomes:UP000199012};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOKA01000002; SFA82506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0W3N4; -.
DR STRING; 988821.SAMN05421867_102114; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000199012; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000199012}.
FT DOMAIN 42..199
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 697..913
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 95147 MW; 8BA1E0A0FC4AEC5E CRC64;
MADVAADGAG AAVPPAGARA PGPGAYPAAW EADVVLYDGS TTHVRPIRPD DAEALQAFHL
GQSERSTYMR WFAPMERLSE RDLTHLVTVD HDDRVALVAV TGGDGPGDDE RITAVARYDR
IDPDVAEVAF NVSDAHQGKG LGSALLEHLA AAARERGVRR FVAEVLPQNG RMIATFREAG
YAVRQHTEDG VVSVEFDIDP TERSLEVMAD REHRAEARSV RGMLGARSVV VVGPGSGATG
VTVRLAQTVT GALRAGDPTL PVHTVGVPGR PGEADRWAAL AELPTPVDLA VLAVEAADAE
GFVRALARHG VRACVLLSAG FGETGAQGLD LQRRLLRAAR GTGLRIVGPA SFGLVAVRPD
GSVLDASLVR ETLPRGRVGL FCQSAQVAVG LAGAVRRRGL GVAQFVSAGH RADVSGNDLM
QFWTDDESTD VVALALESIG NPRKFQRIAR RLSATKPVVV VTAGRSGQVV PPGHQVRSTY
APARTLDEMM RHAGVIRVES TGAMLDLVQL LAHQRLPAGR RCAVLAGSAT VAAVVVEAAA
GAGLVVRQDP VVVPEDAGPD AVAAAVEQVY AQDADVVVAV RVPTVYGPDP VLHRAVAEAA
ARTGRPTAAC FTGLSGITAD LTAPGPDGRP CTVPAFGTAE DAALALGRAA RYARRRAEDR
GRPVAPPGVD VRAARRLVRA WSASDGAPVA LDAARTATLL SAVGIGVVPA VPARDAEEAV
RAARAMGYPV ALKTTVPALR HRADLGGVRL DLEDDDEVRA AAAALAAVTQ GQRPAVDEAP
LEVQAMVEQG VSCVLRSTED PLFGPVLSFG VAGDATDLLG DVALAMPPLT DADVAAFVRS
PRAAARLYGY RGSPALDAAA LEDLVARVSL LADGLPELRS LELNPVVVTL DGVRVLGARA
GIGPADRSDA PARALGR
//