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Database: UniProt
Entry: A0A0S1YAD7_9BORD
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ID   A0A0S1YAD7_9BORD        Unreviewed;       705 AA.
AC   A0A0S1YAD7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=6-carboxyhexanoate--CoA ligase {ECO:0000313|EMBL:ALM86929.1};
GN   ORFNames=ASB57_12185 {ECO:0000313|EMBL:ALM86929.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM86929.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM86929.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM86929.1,
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; ALM86929.1; -; Genomic_DNA.
DR   RefSeq; WP_057656102.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1YAD7; -.
DR   STRING; 1746199.ASB57_12185; -.
DR   OrthoDB; 8664175at2; -.
DR   Proteomes; UP000064621; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   Ligase {ECO:0000313|EMBL:ALM86929.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT   DOMAIN          491..703
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   705 AA;  73140 MW;  2E30C605D7C3C929 CRC64;
     MDAINRLLNP RSVAVIGASA DVKKTAGRPV AYLLKHGYAG DIYPVNPRAD SIAGLRCYPD
     IASLPAVPDV GIVLLGAERA HLAVRELAER GAAAAIVLAS GYTETGAEGA RRQEELREAA
     GSMRLLGPNT IGLVNLTDSI VLSASGALEM DHFPVGSIGV VSQSGGILGA LLSRAAARGI
     GLSKLISTSN EVDLELADFV DYLADDEATK VIALYVESVR NPEKFRAAAL KAARAGKPVV
     AFKIGRSEAG AKAAVSHTGA LAGADRMYDA LFKQVGVIRA QTFGDLLDIP VALATDRKLR
     GNRVAILTST GGAGTLVSDS LGVSGFDTPP PDAETGARLR ALQTGDHAAL DRNPIDVTLA
     GLQPDLLRGA IRALLDSPSY DALTIIVGSS SLAMPELMAG AIQDCLPESD KPVIAFVSPH
     APAVGALLTQ RGVPAFAAAE SCTVALAGML QHANWKAHSS PAVPAPVDVR DLLPAMAPGK
     ETVSLNEAEA KQLFARFDVP CAGETIVTTP EEAERAARAY GGRVVLKILT GAITHKSDVG
     GVAVNLAPEQ VGARLTAMQA EVKDKTGILP ERFLVQEMVA GGTELILGMH RDPLGTAILL
     GMGGITAELF KDTTMRLLPA DGRGLSAEEA LEMVRELKTW PLLDGYRGRP KADVQALVAA
     IVAFARMTAQ LGDRLVEAEI NPVFVLPEGQ GVRAADGVVV LGAAA
//
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