ID   A0A1W6YPF5_9BORD        Unreviewed;       692 AA.
AC   A0A1W6YPF5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=CoA-binding protein {ECO:0000313|EMBL:ARP82965.1};
GN   ORFNames=CAL12_20520 {ECO:0000313|EMBL:ARP82965.1};
OS   Bordetella genomosp. 8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP82965.1, ECO:0000313|Proteomes:UP000194151};
RN   [1] {ECO:0000313|EMBL:ARP82965.1, ECO:0000313|Proteomes:UP000194151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU19157 {ECO:0000313|EMBL:ARP82965.1,
RC   ECO:0000313|Proteomes:UP000194151};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021108; ARP82965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6YPF5; -.
DR   STRING; 1416806.CAL12_20520; -.
DR   OrthoDB; 8664175at2; -.
DR   Proteomes; UP000194151; Chromosome.
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          8..103
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   692 AA;  73245 MW;  C70AFF7CDEFDDC72 CRC64;
     MNDNFEYLFA PNSVAIIGAS DNPNKIGGRP IHFLRKYGFR GDVYPVNPGR QMVQGYRAYS
     DILDVPSVPD SVVIAVGTDA VADQVERCAQ MGVRAAVLMS SGFGELGEKG RARERRLVEI
     ANASGMRLMG PNCQGTANFS NGTILNFSTM FTDVAAQDGP IGIVSQSGAA SVMPFALLRQ
     AGLGVRYVIA TGNDADLGAC AMAEAVARDE DIKLILVYLE QISEPHRLAS AARIAKERGA
     YIVVLKSGGS TKGASAAASH TGAVVGNEAA IDAFLARSGI WRARDIQDFI LAAPLYLSDR
     PVGAGRSVAM SHSGAVAVMT ADLAEREGLE LADLADETKT RLTAILPDFG TAHNPLDTTA
     AVLSDPTMFP RVLSAIGLDS QADTVMVSVP MAGPGYDLET FADAAAEFVR TQNKPMVLSA
     PQPNVRAVFS ARDIPVYATE ADAIRALQQY TKHQQLRAAL RESRVIEPIM GLPRGLQDEH
     RSLSLISDHG VPVVENILCN SPDEAVTAFH ELGNVPVVVK GCAASIPHKS EHDLVYLHIR
     STDDARRAAE SCFAALKDMG ITKPQVLVAK MVKGEHEIAL GATVDAKLGP LVMIADGGTL
     VELRKDAVTL LAPFTAKQAR EALARLRIAP LFQGYRGKPP LDVQALAEAA VALGDFAAGS
     RESLISVDIN PVMVMPSGEG VLAVDAVVEL NQ
//