ID Q7VX74_BORPE Unreviewed; 706 AA.
AC Q7VX74;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Pimeloyl-CoA synthetase {ECO:0000313|EMBL:CAE42215.1};
GN OrderedLocusNames=BP1933 {ECO:0000313|EMBL:CAE42215.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE42215.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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DR EMBL; BX640416; CAE42215.1; -; Genomic_DNA.
DR RefSeq; NP_880617.1; NC_002929.2.
DR RefSeq; WP_010930644.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VX74; -.
DR STRING; 257313.BP1933; -.
DR PaxDb; 257313-BP1933; -.
DR GeneID; 69601718; -.
DR KEGG; bpe:BP1933; -.
DR PATRIC; fig|257313.5.peg.2077; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_4; -.
DR Proteomes; UP000002676; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000002676}.
FT DOMAIN 21..116
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 706 AA; 73907 MW; 9C6E2BE692F12516 CRC64;
MSTLADNAPR MAGAGDWIDA ALAPRSVAIV GASDNPEKIG GRPIKYMLQH GYQGRILPIN
PGRDRVQGIA AWHSLDAVNV PIDMLLVCVA GEAAVQAVRD GARLGVRVCV VISSGFAETG
EPGRQAQKHM KAAAAAAGMR LLGPNTQGLA NFSNGALATF ATLLGEVAPA DGPVAVISQS
GAMSMVPYAH LRAEGIGVRY SVATGNECDL NVADFTEAVL RDPEVRLILL YMESLPAPAT
LARAAALARS RQVPVLALKA GVSPQGLQAA QSHTGAIATE DKALDAWFRQ HGILRVPDAR
SLVMGAQLLL RCGHLPGNRL AILSNSGAAC VTGADAAERH GLQVPPLPAE TRARIDAVLP
GFASSLNPID LTAALLSNNH LFGQVLPILA SARACDALFI TLPMSGKGYD TDQFARDAAA
FTAETGLPVV VSCPLAASRR IFAQAGLATF EHDEDALAAL GQLARLSGLR ETALRLARPA
PHAPAAPVPR TAGLLSEADS LEQIEAIGIR TAPWRLCLDA DSMGSALGSL PGPWAVKACS
AQIPHKSEYG LVHLGIADEQ RARALFPVLR QEVLGMGKSF DGVIVASMVK PRREFMIGAR
WDSQFGCIVI VGDGGKYVEA MPDVATLVYP FDQAHAEECL RKLRVAALFD GVRGENPLPV
QELAHAATRL GAWLHAQQGA VASVDINPLI AGPDGRLYAA DALVEI
//