ID A0A0S1Y2S5_9BORD Unreviewed; 702 AA.
AC A0A0S1Y2S5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:ALM84241.1};
GN ORFNames=ASB57_15795 {ECO:0000313|EMBL:ALM84241.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM84241.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM84241.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM84241.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013111; ALM84241.1; -; Genomic_DNA.
DR RefSeq; WP_057653085.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y2S5; -.
DR STRING; 1746199.ASB57_15795; -.
DR OrthoDB; 8664175at2; -.
DR Proteomes; UP000064621; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP 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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_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; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_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;
KW Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT DOMAIN 7..102
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 702 AA; 73663 MW; BA2F4DD0EFA8CA31 CRC64;
MSKFKHLLEP RSIAIVGVSD EAGRPGSQAL RALRANGYTG ALYPVNPKYQ EFDGLKCYPS
VEAIQEDVDL VIIGVPAKAV LPVMENCAAK RVGYALILSG GFRESGAEGI ERERAIIEVA
RQSGMRLVGP NCLGFANIHA GVFAAFGSIT REPKLAHGQV SLVTQSGGFG YSIALACAEE
GIGFRHVIAT GNEADIDSVE FIDSLIDDDE TKCIVVYIEG TRDGRRLLAA GQRALAAGKP
ILLWKGGVTD EGARAAESHT ASMTGTYDFY RALYKQTGII EITELHEIVD YLKLLQAEKH
LERGGVGVLG VSGGSAIVFA DAGARQGLSL CELASVTQER LAPVVPSIGA IHNPIDLTAG
YFSAGNEEKL ETAIRAVLED GGVGAVCVNL ATTGAQGSTV AAQVLTRVAQ DYTKPVVVFS
STPRAINGDA RAIFAKGNVP VFPSPSRAAN ALGMLLRLGQ AKQRLRVGAV DYAAATGIEP
GAVFSEIDSK EILARAGVAV TRDLLLAAGQ TPDLQGFRYP AVVKIVSRDI AHKSEVGGVK
LGLRSEAEVH DAIAEVLANA ARLVPSARID GVLVSEMVRG GFELIAGSVN DEVFGPVIMI
GAGGIYAEIL KDVTYRLAPF DAATAAEMLD ELRCRPIFDG ARGGAHLDVG AAAKALAALS
RFAWANRETV QEVDVNPLFL ASDGVVAADA LVVTRKPDVT VS
//
