ID A0A0J1D389_9BURK Unreviewed; 709 AA.
AC A0A0J1D389;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=EOS_05680 {ECO:0000313|EMBL:KLU27180.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU27180.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU27180.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU27180.1}.
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DR EMBL; AEJF01000051; KLU27180.1; -; Genomic_DNA.
DR RefSeq; WP_047845631.1; NZ_AEJF01000051.1.
DR AlphaFoldDB; A0A0J1D389; -.
DR PATRIC; fig|908627.4.peg.1251; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000035963; Unassembled WGS sequence.
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; 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; 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.
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 494..530
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 709 AA; 75194 MW; 1DC400806DCD9766 CRC64;
MNDLADYSQT SIHAMLHPRS IALIGATPRM HYGGKFLKRL LAYRDRVEVY PINPKYNEIM
DQPCQPSITS LAQAPDLAVI IVPWHAVLQT MQECSEKGVK AGIVISAGFS ERGTDERRGL
QKEIGRFARA SGFRITGPNC LGLANIHDDL WLTSSSRVLT GSAGPIGLIC QSGATLFGPL
LARAADNGIG LSYAISTGNE ADLEFADFAR YLLDDPGTKV IAGFIEGFKD ANKFVQVAKL
AAERGKPLVI IKIGRSEQGA RAAGSHTAAL TGSDALYDAV CKQYGVIRVT NYDELLDISQ
VLAHFKLQRR DGVAVVSHSG GVSSLTADML GNDGITLPAL SPNAESTINA ILNGFGAASN
PADITGKANS EEFPAIIGAL ADEEEIGTLV VASAGGDRHA EQLIALRDTT DKNVAYLWTG
SRAQETGLPK LKAAGIPIMS NPDGLAKALR AAFDYHAWRE QRVASQAASK SSASECLDPF
VRQGRTTLTE SEGKQLLREW GIASPRERLV SSASEAAAAA QEIGFPVVMK IDSPDIQHKT
EAGGVKLDVR DAQSSQSAFD EITSSAMRYA PDARINGVVV QEMVSGGVEM IVGITYDAQL
GATLLVGSGG VMVEVFKDVA LRQCPVSRHE AMRMIDDLKG SVLLRGFRGS PPADTDALAD
ALVEISQVAM QCNGKLAEMD INPLLVLPAG EGVRALDALI TLCSAGNLI
//
