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Database: UniProt
Entry: A0A0M8WHJ3_9ACTN
LinkDB: A0A0M8WHJ3_9ACTN
Original site: A0A0M8WHJ3_9ACTN 
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
//
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