ID A0A060QJ23_9PROT Unreviewed; 1331 AA.
AC A0A060QJ23;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:CDG41169.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:CDG41169.1};
GN ORFNames=ASAP_3124 {ECO:0000313|EMBL:CDG41169.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG41169.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG41169.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG41169.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG41169.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG41169.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:CDG41169.1}.
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DR EMBL; CBLX010000027; CDG41169.1; -; Genomic_DNA.
DR RefSeq; WP_023979489.1; NZ_CBLX010000027.1.
DR eggNOG; COG1020; Bacteria.
DR Proteomes; UP000027583; Unassembled WGS sequence.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CDG41169.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 968..1042
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1331 AA; 144921 MW; 4E084A385E02375A CRC64;
MLHKNRAETL PLTTAQRGLW MTQFLAPSGS SLNIAEAIHL RGELRTDLFI ESLTCVQAEA
ETLRTAIVRK PEGPVYTIRP PGSVACPVIA FHDMPDPEQS ARDWMLERLR APLDLEHDPL
WQNALLRLSD TYHIWFHCCH HAVLDGFAGG MVAARVAAHY TARYAGISPP EAAFLPLSTL
HEQEQAYRQS PRFEKDKAYW SEALSEAPEP VSLSLRPQRA PSGEAGGAIT RAAFMSDERA
ESLTRIGRAL EATLPQTLTA LLVAYLYRVT GQSDLVVGMP VSARANRQLR QTPGMVANAV
ALRFRIAPKT SFADLVGMAR RAMRNALRHQ QYRYEDMRRD LGLFSNTTQI SRIGINIEPF
DYNLSFGPIT ARNENLSNGA MEDLTIFVFD RKDGAGLCFQ CDANPALYAT HELDAHLTRI
LRLAEQIANV PDTTLDHLSL LTPEERAAQE ARNRTTRRDW PTTPLTKLID KGVGHGSGPL
VSDAYGVMTR EVFLRQSRAL AEQLRAEGIG PGKLVALALP RDRRMILAVA AVLQAGAAWL
PLDIASPQAR AKLILEDAEP SAVIVPDAAH IDWAAEYTAW ALTSETSTLQ RLSRGKTASS
SPVPDDTAYV TYTSGTTGRP KGVVVPRKAL TNFLHAITER LAYSARETLL AVTAWTFDIA
VLEMLLPLTS GGACVIASRE DILEPGRLAA LVREHGITAM QATPTLWQTL LGTAESSALQ
GMMLMSGGEA MPAHMARQML HLGRAVHNLY GPTETTIWST THHLDPQETD TPAAGHALAN
TQLYIIGPDQ TPLPDGVIGE LLIAGDGVAT GYLNQPELTS SRFIPDPLGV PGRKAYRTGD
RAAIGHDGTL TVLGRGDQQI KIRGMRIEPS EIESTLLSLP EILQAAVMIE KDPARGAPLL
AAYLVPATHG ARLDPSQIRR TLLGLLPPQM IPVRIVCVET LPRMTSGKLD RAALASLREE
TETTTFTEAR TPAERRLSAL WGELLELERV DIHTSFFELG GDSLMVVQMI ACLSREGYAL
PVGQVFAAPT IVLLAPLLEG GSVTCDPLAP CLAIRAQGQN APVFCFHPVI GMSWNFNTLA
PLLSESHPVY GLQDAGLLLK DDAPATLAAL AAFYVAELRR LQPHGPYHLV GWSMGGVVAH
EIASLLRQEG EDIALLAMLD SYPCLLQDQS LAPDSPQAIR AVLQFLQIAP VEDAALPDTL
DGLADLFLET LDTTVLPDLP EIDLNALTSL AEKLRLITRR NIEMLLAHVP TPNDADILFL
RAADKGNQNE VTIVSDDPYA WRAYSSGHIT AHDLDCRHGD MLLPGHVETV ARWINISLAQ
DRTPASCLSA A
//