ID Q6FBA3_ACIAD Unreviewed; 701 AA.
AC Q6FBA3;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Pimeloyl-CoA synthetase {ECO:0000313|EMBL:CAG68660.1};
DE EC=6.2.1.14 {ECO:0000313|EMBL:CAG68660.1};
GN Name=pauA {ECO:0000313|EMBL:CAG68660.1};
GN OrderedLocusNames=ACIAD1826 {ECO:0000313|EMBL:CAG68660.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68660.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG68660.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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DR EMBL; CR543861; CAG68660.1; -; Genomic_DNA.
DR RefSeq; WP_004926963.1; NC_005966.1.
DR AlphaFoldDB; Q6FBA3; -.
DR STRING; 202950.GCA_001485005_03240; -.
DR GeneID; 45234204; -.
DR KEGG; aci:ACIAD1826; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_6; -.
DR OrthoDB; 9807426at2; -.
DR BioCyc; ASP62977:ACIAD_RS08420-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IEA:UniProtKB-EC.
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; 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:CAG68660.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430}.
FT DOMAIN 488..524
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 701 AA; 75053 MW; E65EABB0EED7A6BF CRC64;
MSQSLLDALL NPASVALIGA SDNPARIGGR PLRYLKESGF EGEIFPVNPN RDRVQGMLAY
ADLASLPKAA DVALLAVPAS ATVQAVRECA QKGIQTAIVF SAGFAEAGED GHQMQQEMLN
AAKESNLRLL GPNCLGVFNA YKKFYGTFST VLDGDFIEPG AVSIVSQSGA YGSHIAHLCR
QRGLGIGYWV TTGNECDIDL SDALNWVVDQ PEVKVVLAYA EGIRHRDRFI QALEKAQRNN
VAIIFMKVGR SEVGAKAASS HTAALAGSNA VFDAVLRQYG VIRAKTTTEQ IDIAYAVTRA
GHIEHNRLGV FTFSGGFGIQ MADDAEAAGL DVAPMPEAAQ DELKQLLPYA SPVNPVDATA
QALTDLPMMT SFIQTMLKKG DYQFFAGILG SGPTSPTFAT ALRQTFEEAT KDAPSCLKCL
TMTAPPEIVR QYEEKGFLVY EDGAALINAL GALVKLQQAR TATRSSSDFK LPERIEIPQR
EMNEFAAKQI LKQAGIPCLP EILIAPDDDP TLAANELGYP LVMKIASADL PHKTEVGGIR
LNLKSAQEVS DAKANMLRHV QQLAPSAQLD GVILTPMLKG GRETIVGVFN DQSFGPVVMF
GLGGIFVEVL KDVTFRIAPF GIDQAKAMIA EIKGYALLQG VRGEQPADID ALAKLLSTLS
EFAAVHADQF DSIDLNPVLV LDQDQGVIAL DALIVPRSAQ P
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