ID W6TS95_9SPHI Unreviewed; 2192 AA.
AC W6TS95;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Amino acid adenylation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=N824_22385 {ECO:0000313|EMBL:ETZ22625.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ22625.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ22625.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ22625.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
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:ETZ22625.1}.
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DR EMBL; AWRU01000009; ETZ22625.1; -; Genomic_DNA.
DR RefSeq; WP_048905108.1; NZ_AWRU01000009.1.
DR STRING; 509635.N824_22385; -.
DR PATRIC; fig|509635.5.peg.2194; -.
DR eggNOG; COG0001; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000019145; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 521..596
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 612..1036
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1508..1586
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2192 AA; 242151 MW; ED668F051D29949D CRC64;
MFKDQISNIQ NKLTVHQLFN IAAQDFPEIT AIVFGEKSIT YRELNNRAEN LATIILNQAF
DQQIIGISAT RSIEMIVGLL AILKAGKTYL PLDSSYPENR LLQIIEDSGV STCIALLKES
NIFTGLGLDV IISDKSYADT TKNDNFLQSE NGCILYTSGS TGKPKGVCIS HKSLIHFLQW
QKDHALNGKG INALQFCHLS FDASFQEIFV PLTTGATLYL INEDYRLDGA KLLDFIISNN
INKAFLPYVT LQYLTEAATK EQRFPANLKE LITGGELLKI TPNIREFFSS ISNSSLVNVY
GPTETTIWVT ELKLTGDPDK WASIPTIGET IAQSSIYFID EKSTFLENGQ TGEICISGAC
LSNGYFHQPE LTNEKFIELT HPTLGQIKVY RTGDLGKLLD NGEIEFEGRK DGQVKIRGNR
VELGEIEVAL MKEESVNQAI VILREDYPGR KAIIAYLTGN DATGDSNKLR YHISKLLPDY
MIPSGFIWLN ELPKTTSGKV DRKALPKPDL KRPELNVLYK SPKTKIEKDV TGLFLDIFQY
DKIGIEDNFF ELGGNSLLAQ KTIAELKYQF SYHLPITKLY QYPTVAGIAE FLEKKSPEQV
SSAKLGAYSN DSQDIAVIGM AGRFPGAETI EDLWGLLIEG KETTKFFSDE ELDISIPDRI
KNDKAYVKAR GVIKDAEKFD PAFFGINTKL ADLMDPQQRI FLEIAWEVLE KTGHLFPVYP
KKVAVYAGSG SNTYYVNNLL QYPDLIENQG SLQVLTVNEK DYIASRTAYH LNLKGQAVSV
NSACSTSLLA IVEAVNSLRS GQCDAAIAGA SSITSPINSG HIYQEGSMLS ADGHCRPFDN
DATGTVFSDG AGVVLLKRLS DAKRDGDVVY GVIKGVGLNN DGAEKGSFTA PNTEGQANAI
KQAITDAGID ASAISYIETH GTGTPIGDPI EFDGLVEAFG HQNKTQFCAI GSVKSNFGHL
TQAAGVTGLI KACLSLHHKK IPASLGYKQG NKNIDFLNSP FYVNNSLSDW TCETKRIAGV
SSFGVGGTNV HVIVEEYENL EPKSSTGRPY DLITWSAKSE NSREQYGSSI ADYVKKNKDI
NISDIAYTLQ KTRNDFSYRR FAVVNNTESI ISQHHLELPK TGSINNLREM PEEVVFTFPG
QGAQYLNMAA DLYKDEPIFR EAVDHCSEIL KQYIDLDIKE IIFTNSVDEK AEQLLKETRY
TQPALFVIEY ALARLWMNWG ITPTLLCGHS IGEYVAAHLS GIFSLEDGLK LIATRGAMVN
ALAAGSMLSV RSESDLVSSL LSKGLCVAAV NSPKLCVIAG PEDQILQFSK LLDTKEIPNK
LLFTSHAFHS SMMDPIVDDF QKVVSEISLS VPQTPIISTV TGVVLTNEEA TDPQYWASHL
RNTVQFSKAI ETALTYNSPI FLEVGPGSVT TTLVRQIAAL KSTPVRGMQS LSNNENDYCI
ILNTLGQLWN YGLQPNWDNF YHNQKRSFLD LPTYQFDRKR HWVDAVAINK VIPEDDSNKP
NTNNTLAMKK NNLAIKIRQV LEDASGIEMQ NVESNQNFLE IGLDSLLLTQ IAISLKREFN
LPITFRKLNE EYSTIELLTD YIENNTVQQS PESTQNSNPV VHVNNHQVIA PVSFGNAIDY
NNSALGLIAQ QLEILSKQVL LMNGNNPVAA PIAIQPSKPV QQEESELTVQ EKSEIQKPFG
ATPKIDRQST ELNKDQLSFL EKLIERYNHK TFKSKKYAEE SRNYMADPRV VSGFKPLTKE
LTYPIVINKS SGSRMWDLDG NEYIDVLNGF GSNLLGYQPE VIKKAMHDQI ENGYEVGPQH
ELAAEVSKLV CEFTGFDRSA LCSTGSEAVL GCIRIARTVT GRSLIVAFTG SYHGIIDEVL
VRGTKKLKSF PAAAGIMPDA VKNILVLDYG TEEALAIIKE KADEIAAVLI EPIQSRRPEF
VPIDFVKEVR KITSASGSAL IFDEVITGFR MHPGGAQALF NVRADLASYG KVVGAGIPIG
VIAGKKEYMD ALDGGTWSYG DSSYPEVGVT YFAGTFVRHP LALASAKASL LYMKEKGPKL
QLELNEKGDY IAKTINKEIE KRHLPFFVAN YGSLWKVKFN EEIPYSELMF TLMRQKGIHI
LDGFPCFVTE ATSNSDIEQV INCFVESMDE MIAAGFFPSS GGSDVKFNPQ AIVISADTPP
IDGARLGKDK TGNPAWFIKD PKNGKYLQLG FN
//
