ID   A0A261SL07_9BORD        Unreviewed;       709 AA.
AC   A0A261SL07;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Pimeloyl-CoA synthetase {ECO:0000313|EMBL:OZI38086.1};
GN   ORFNames=CAL29_07005 {ECO:0000313|EMBL:OZI38086.1};
OS   Bordetella genomosp. 10.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416804 {ECO:0000313|EMBL:OZI38086.1, ECO:0000313|Proteomes:UP000216020};
RN   [1] {ECO:0000313|EMBL:OZI38086.1, ECO:0000313|Proteomes:UP000216020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU16122 {ECO:0000313|EMBL:OZI38086.1,
RC   ECO:0000313|Proteomes:UP000216020};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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:OZI38086.1}.
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DR   EMBL; NEVM01000001; OZI38086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SL07; -.
DR   OrthoDB; 8664175at2; -.
DR   Proteomes; UP000216020; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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.
PE   4: Predicted;
FT   DOMAIN          19..114
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   709 AA;  74914 MW;  5B92FAEDD42770CC CRC64;
     MQAVMPAPAR AREAWIDAAL NPRSIAIIGA SDNPDKIGGR PIKYMLQHKY AGALYPVNAA
     REQVQGIRAW PDIAALPETP DMALVCVPGA AALEAVTQCS QRGVKVCIVI SSGFGETGAE
     GLAVQRRMAE VAAASGMRLV GPNSQGLASF DSNALATFAT LLGEVPPQDG PVAIASQSGA
     MSMVPYALLL AQGIGVRYAF ATGNEADLTV ADFACAAAED PAVRLILLYL EDLVDPDTLT
     EAARLARQRG IPMLALKAGV SDRGQAAALS HTGAVATEDK VLDAWFRQNG ILRVAEMRSL
     VQGARLLLKP RRLKGRRVAV LSNSGAACVM GADAAERHGL DVPPLPDDVR QTIAKLLPNF
     ASAQNPIDLT AALLTNNRFF GDVLPHLAGD CCDALFISLP MSGQGYDAEQ FARDTAAFQA
     DSGKPVVLAC PLRRTREVFE SHGVVAYEHD EDAMAALGQL AAVSALQSEA GRLAEAGSRA
     RHPAGVPAET TRFLSEADSL EQLEAIGIPT APWRLCKTDE DVRLAMRTLA LPVVIKACSA
     DIPHKSEYGL VKLGIGDADE ACAIAGEMRA TCGRLGKSLD GIIVASMVRG RRELLIGARW
     DEKFGSVLLV GDGGKYVEAM PDAVTLVQPF DLSHVLRQLR TLRLAPLFKE TRGDPPLPVE
     ALARLAVVVG NWVQAENGRI ISVDINPLMA QPHGGLVAAD ALVEINGRQ
//