ID C5T924_ACIDE Unreviewed; 542 AA.
AC C5T924;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cyclohexanecarboxylate-CoA ligase {ECO:0000313|EMBL:EER59030.1};
DE Flags: Fragment;
GN ORFNames=AcdelDRAFT_3404 {ECO:0000313|EMBL:EER59030.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER59030.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER59030.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER59030.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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:EER59030.1}.
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DR EMBL; ACQT01000171; EER59030.1; -; Genomic_DNA.
DR RefSeq; WP_005798924.1; NZ_ACQT01000171.1.
DR AlphaFoldDB; C5T924; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000003856; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05903; CHC_CoA_lg; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR017621; Cyclohxane-COOH-CoA_Ligase.
DR NCBIfam; TIGR03208; cyc_hxne_CoA_lg; 1.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EER59030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856}.
FT DOMAIN 33..407
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 456..532
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT NON_TER 542
FT /evidence="ECO:0000313|EMBL:EER59030.1"
SQ SEQUENCE 542 AA; 58967 MW; 820B6B85140DBF26 CRC64;
MEFDAVLLPP RRARMVAQGH WHDRTINDAL DACVAACPDK AALTAVQIEA GTTTRFTYRE
LARMADRIAV GLARLGVGRG DIVACQLPNW WQFTLTYLAC SRIGAVMNPL MHIFRERELS
FMLQHGEAKV VIAPQIFRGF DFEKMITGLQ PSLPHLKHVV VVGGSGANSF DALLSGPAWE
QQPDAQAILT AHRPSPDDVT QLIYTSGTTG EPKGVMHSAN TVMSNIIPYA ERLHLGAEDV
VLMASPMAHQ TGFMYGLIMP ILLQASAVLQ DIWEPAKAVA LINAEKASFT MASTPFLTDL
ARTVAETGVA VPSLRTFLCA GAPIPGPLVE QARKALGAKI VSAWGMTENG AVTLTRLDDD
DERSFNTDGC PLPGVEIKVV DVDGQPLPPG QPGKLLLRAC SNFGGYLHRP HLNATDADDW
FDTGDLARID ERGYLRITGR SKDVIIRGGE NIPVVEVESL LYRHPAIALA AVVAYPDERL
GERACAVVVP KPGQTVDLPG LVQFLKEQRI AVQYIPERLI VRDAMPSTPS GKIQKFKLRE
ML
//
