ID A0A0M8WHJ3_9ACTN Unreviewed; 754 AA.
AC A0A0M8WHJ3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Pimeloyl-CoA synthetase {ECO:0000313|EMBL:KOV85820.1};
GN ORFNames=ADL01_08060 {ECO:0000313|EMBL:KOV85820.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV85820.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV85820.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV85820.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV85820.1}.
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DR EMBL; LGDW01000054; KOV85820.1; -; Genomic_DNA.
DR RefSeq; WP_053741209.1; NZ_LGDW01000054.1.
DR AlphaFoldDB; A0A0M8WHJ3; -.
DR PATRIC; fig|1519490.3.peg.1759; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000037738; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
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; 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; 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.
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:UP000037738}.
FT DOMAIN 534..574
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 754 AA; 80234 MW; 945F435445BC1F98 CRC64;
MLGSTHGTLT TTSRRARVIA CGEQPSPVVH GRPADVDDLD VSGRPLYAGV PDLDRFFRPQ
SLAVIGASDA EGRPNTGITR QLLAWAERVG ARLHPVHPTR EAVFGIPCFP SVADLPEQVD
LAVLLVADPL PLVEQLAEAK VRFAVAFASG FAETGEAGAE AQARLSAAVR RSGLRLLGPN
TNLNAFENFR EDLDGPAIAL ITQSGHQGRP VFALQELGIR LSHWAPTGNE ADLETADFIS
YFSERPEVGA IACYVEGLKD GRSFLLAADR AARRGVPVVA VKVGRTETGA RTAASHTGKL
TGADTVVDAA MRQYGVIRVD GLDQLQDTSA LLARARRPLA DGVAVYSISG GTGAHFADLA
TEAGLNLPQL SAAKQAELHE WIPDYLNVAN PVDSGGHPVG DWRGRKIIDA ILADPAVGVL
VCPITGPFPP MSDKLAQDLV DAAEQTDKLV CVIWGSPVGT ESAYRETLLG SSRVATFRTF
ANCVTAVRAH LDHARFTASY RSPFDEAPRT PSPSFRKARA LMRPGEALSE HAAKLLLRAY
GIRVPREQLV TSAAAAVRAA GLVGYPVVMK ASGGQIAHKT ELGLVKIELT SASQVRDAYR
ELTDIARYEG VDLDGVLVCQ MVERGVEMVV GVTHDDLFGP TVTVGLGGVL VEVLRDTAVR
VPPFGEEQAR DMLTELRGRP LLDGVRGRPP ADLDALVEVV LRVQRMALEL GDELAELDIN
PLMVLPRGQG AVALDALAVC GPGPENQDVN QQPL
//