ID A9ISQ2_BORPD Unreviewed; 1113 AA.
AC A9ISQ2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:CAP43329.1};
GN OrderedLocusNames=Bpet2987 {ECO:0000313|EMBL:CAP43329.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP43329.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP43329.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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DR EMBL; AM902716; CAP43329.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ISQ2; -.
DR STRING; 94624.Bpet2987; -.
DR KEGG; bpt:Bpet2987; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR eggNOG; COG5361; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.60.120.600; Domain of unknown function DUF1214, C-terminal domain; 1.
DR Gene3D; 2.60.40.1610; Domain of unknown function DUF1254; 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; IPR010621; DUF1214.
DR InterPro; IPR037049; DUF1214_C_sf.
DR InterPro; IPR010679; DUF1254.
DR InterPro; IPR037050; DUF1254_sf.
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; PF06742; DUF1214; 1.
DR Pfam; PF06863; DUF1254; 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.
DR SUPFAM; SSF160935; VPA0735-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 487..523
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1113 AA; 117500 MW; 04936F3ABFBBC5CB CRC64;
MMLSDLDSFL SPRSIAIVGA SSQPGKVGAV PVRYLVEHGY HGEVYPINAG ARQVQGLAAF
ASLRAVGRPI DLAIFAIPAS GADAALDDAI AAGVRNIVMF SAGFAELGEQ GVAAQSAFAA
KARAAGIRVL GPNCLGFMNV ARSVYATFSP VVSTGRVEAG PVGLVSQSGA FGAYAYAMAR
ERGVGLSMWV TTGNESDIDV ADCIAWMARD PATRVIMAYL EGCRDGAKLR QALELARAAG
KPVVAVKVGR TALGAQAAAS HTAALAGDDA VYQTLFRQHG AWRARTIEEF FDIAHCLAVS
GRPANTRVGL LTVSGGVGVM MADDAAEAGL DVAELPAAAQ AIIRARVPFA ATQNPVDLTG
QVTADPSLLE TAARAMLEQG GYGSLLIFLA AFGSTPAMQA MQQQLARDLR RDFPGRLVMF
SALADAAQQR ALEAQGCLCY GDPARAIRVL AALAFFHDRQ QRPAAELAVA APPVALRPGA
YHEAEALQVL RDSGLPVTPA RHAQSRDEAL RHARALGFPV VMKVVSADIT HKSDVGGVVL
DIRDEDAAAH AYDRILAAVA KAAPQARTQG VLVAPMVRGG VECILGARRD PVLGPVVMVG
AGGVNVELLG DVALRLAPVT IEQAREMIGE LKAAALLRGF RGAPAADVAA LAEAIVRLSR
FAMAAGDTLD SVELNPLAVL PEGQGALALD AVLLARAVPT AASAARQAVI ATLPLFEMAR
MRASNTARKH AVAGYAGDSP ASRMRWVNQF THTRRLRGPD DKEVVTPNND TLFTNAWLDL
SAGPLVIDVP EMGTRYWVLG FLDAWTNPWA YAGRRTTGGA AQRLFVHGPG WRGAVPAGMH
PIVAPSDDVW VIGRILVDAD PADLARVHAL QDQFAIRRPD GTPALSRIDV LLDNRDTGVP
DAGEYLRVLG SMLERNPPAA ALPGWPPAVA ELQTALAEVY TELRDVAQPS ELGGGWTTAV
AVRTSFGADF LTRARVARNW IGTLGIDEAM YIMAEVDAQG EPLTGARRYV LRFPPQGGPR
VGAFWSITLY RRSDCLLAAN PIGRHSIGDR TPGLQYDADG GLSISIQADD PGAAKNWLPA
PAGEGFYLTL RLYQPEPDHL EGRFDYPPVR RVE
//
