ID F7VH29_9PROT Unreviewed; 1355 AA.
AC F7VH29;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:GAA09674.1};
GN ORFNames=ATPR_2678 {ECO:0000313|EMBL:GAA09674.1};
OS Acetobacter tropicalis NBRC 101654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA09674.1, ECO:0000313|Proteomes:UP000004319};
RN [1] {ECO:0000313|EMBL:GAA09674.1, ECO:0000313|Proteomes:UP000004319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA09674.1,
RC ECO:0000313|Proteomes:UP000004319};
RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA Yakushi T., Matsushita K.;
RT "Increased number of Arginine-based salt bridges contributes to the
RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT tropicalis SKU1100.";
RL Biochem. Biophys. Res. Commun. 409:120-124(2011).
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:GAA09674.1}.
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DR EMBL; BABS01000111; GAA09674.1; -; Genomic_DNA.
DR Proteomes; UP000004319; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic 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; 3.40.50.980; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 991..1065
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1355 AA; 146991 MW; 6317EE5F909730CD CRC64;
MRFDTGSLSL QTVPETRLPL TTAQRGVWMG ILLRTQGGTF NIAEAVEILG PVDPALFRAA
LVQVAQEAET TRVSIRMGAD GPYQVILPTL RCPLPFVDFS TRPDAAAQAQ HWMMARISQP
VDLAEDPLWT SALIKLSADS FIWFHCCHHI ALDGFSGGLI VARVAELYNA MVEGREPAPC
TFLPLERLVA QEAAYRTSPR REKDQAYWQH QLAAPPEAVT LASPLPPSVP EAPLQRLGFV
ERNVLVPPAM VGQMQGLAQQ AGVTLPQMLT ALLSTYIFRM TGQEDLTLGM PVTGRTDREM
RRVPGMAANA VVLRFAMAYT LGFSEILLQA RRALHGALRH QAFRYEDLRR VLGFHDTQQH
LSRIGINIEP FDYHLSFGGS PARNRNLSNG VMEDLTFFVF DRQDGQGLSL CLYANPTLYD
GPALERHLRH VMRLIKAILA DPAQPIGAYP LLDAAEGKAL LADETATASN WGPRALVADL
ARHAAYAPTA TALTDGRGPV SYAALLHAAQ GLAKHLMACG IGPGDVVGLM LPRDRRQVIG
MLATMAAGAA WLSLDRCGPR ERNAAIIANA RPALFLTEDT LPTGLPDGSA VLGLAEDGAP
ATVFSNPDAQ RAPVVPQGTA YVIYTSGTTG TPKGVVVPWS ALTNLLCTMQ DKLALGAQEC
WLSVTSVTFD ISILELLLPL QAGAHLVLAR RETVTDPTLL SAIVQHYGVT LMQATPTLWQ
MLVGAGQGRC LAQVRVLSGG EPLPVSLART LQKHARAVYN VYGPTETTIW STFHAVTAED
GSRGQPIPAG RPLANTQCYV LDPAGGLLPV GTPGQLAIAG AGVATGYLDR PDLTHAVFRP
DPFSKIPHAR LYLTGDRAVR QPDGTITVLG RTDAQIKIKG VRAEPAEIEA ALLTLPGIVQ
AAVRVWPKAQ GPVLVAYLVP AAAAQAETIT PEEEAQNFAL FRTHLQGLLP AQMVPSRFVV
LAALPLTASG KLNRKMLPEP EDAEHIPQHE SPQTAQEQLL FTLWSDILDR KDFGINENFF
DLGGDSLAAV QVATALTEQG YELPVASLFG APTIARLAPL LQHQHVVPDV FEETVVPLRA
EGTGQPIFCF PPILGVSLGF TALLPHLPAE RPVYGLQDMG LLHGPQRPQT IQQLAELYLE
QIRALQPHGP YSFVGWSMGG LVAHAVAARL MAEGEPLSAL VMLDTYPLHD PAALEAGQDL
ARMDDTWLVK NAIAMLGIDF SENMPETLDD LADRIVEIML PEAQAFVQDE AAFSTLLQTI
RQGVSHNLEM MRNWQPQRVQ ADLLFLRATQ RGTEDVGDNP AFWQNYITGK LMVTDINCTH
MEMLAPENAL VIADRFMAFE RRKPDRLKGC LNSQQ
//
