ID A0A1H9XQY0_9PSEU Unreviewed; 892 AA.
AC A0A1H9XQY0;
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:SES48560.1};
GN ORFNames=SAMN04487818_12031 {ECO:0000313|EMBL:SES48560.1};
OS Actinokineospora terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155974 {ECO:0000313|EMBL:SES48560.1, ECO:0000313|Proteomes:UP000199051};
RN [1] {ECO:0000313|EMBL:SES48560.1, ECO:0000313|Proteomes:UP000199051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44260 {ECO:0000313|EMBL:SES48560.1,
RC ECO:0000313|Proteomes:UP000199051};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOGI01000020; SES48560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9XQY0; -.
DR STRING; 155974.SAMN04487818_12031; -.
DR Proteomes; UP000199051; 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 CDD; cd04301; NAT_SF; 1.
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 SMART; SM00881; CoA_binding; 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:UP000199051}.
FT DOMAIN 26..179
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 676..714
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 871..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 93293 MW; 86F7456CECBB0702 CRC64;
MADERDPFAY PPQWEADVVL SDGGTVHLRP IVPSDAEALR AFHGRLSERT RYFRYFGPYP
MIPDKDLARF STVDHHDRVA FVALLGDDIV AVGRYERLPG GDSAEVAFVV QDGHQGRGLG
SILLEHLAAA ARERGVGRFE AEVLAENAQM VRVFRDAGYQ VSRAFDEGVL HLEFAVDLTE
ASVAVAWSRE QAAEARSVHN LLHPRSVAVI GASTDRAKIG NAVLGNLLAA DFTGPVFPVN
PEHKSVRGVR AYPTVLDIPD PVDLAVVAVP AAGVDEVMDA CLAKGVKTLV VVSSGFGETG
PGGRGAERRL VDEARAHGMR VVGPNALGVV NLDPAVRLNA TLAPTLPGPG RTGFFCQSGA
LGTAILADAA ARGLGLSTFV SAGNRADVSG NDLLQYWETD PATDVVLLYL ESFGNPRKFA
RLARRLGRSK PVVVVKSGRN TVLPALAKTG VAVDDASVQA LFEQAGVIRV ESIAQLFDTA
LLLAHQPLPP GERVAVVGNS SAIGVLAADA ALGQGLVLAG DPVDVGAQAG PDTFAAAVAD
ALRREEVDAL IVVFVPPLAI PGTTYARALR EAAEGLPEAG TKPIVSTFLA ADGIPAELAV
LGPDGAPTHG SIPSYPSPER AALALARATT YARWRSSPPG IFVRPADIDP AAAKSIVEAA
LTREPTEVEL TDDEVIALLG AYGIEVMPFH VVSDPDAAVA AGAELGLPVV MKTASRQFRH
RSDLVGVRLD LTAEDAIRNA YAELRLVSGV PEVYVQRMAP KGNSCSIGLQ DDPSFGTVVS
FGLAGVVSNL LGDRAYRAVP LTDTDAAGLI RSPRAAPLLA GYAGGEPADL AALQRLVLRV
SAMAEDIPEI RGLMVEPILA SAAGAYVTGG RVTVGPPPSK HDSGPRRLRS SG
//