ID A0A1N6VJW1_9FLAO Unreviewed; 2218 AA.
AC A0A1N6VJW1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SIQ78130.1};
GN ORFNames=SAMN05421797_103160 {ECO:0000313|EMBL:SIQ78130.1};
OS Maribacter ulvicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=228959 {ECO:0000313|EMBL:SIQ78130.1, ECO:0000313|Proteomes:UP000186953};
RN [1] {ECO:0000313|EMBL:SIQ78130.1, ECO:0000313|Proteomes:UP000186953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15366 {ECO:0000313|EMBL:SIQ78130.1,
RC ECO:0000313|Proteomes:UP000186953};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTMA01000003; SIQ78130.1; -; Genomic_DNA.
DR RefSeq; WP_076548550.1; NZ_FTMA01000003.1.
DR STRING; 228959.SAMN05421797_103160; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000186953; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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; 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; 3.40.50.980; -; 2.
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; 3.40.640.10; 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; 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; 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; 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 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 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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 514..589
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 604..1028
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1515..1590
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1669..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2218 AA; 244900 MW; 537A97A55CD38B06 CRC64;
MSSTNQLYLL FEEAARLYPN SVCLINDENI FTYKEAEQKI AAVCHAILDL AKDEKFIGVP
TTRGIEQIIF VLAVLKAGKA YLPIDFKYPK KRIESIIANS KLAYCLTTDT DDTSAKANGL
TPIKIVSDKE TTHQHTTSTT TNNLATYILY TSGSTGEPKG VCMGENALLN LINWQNKHSI
NKNGSRTLQF APLSFDVSFQ EIMATLSNGG TLVLINEEQR LDMVALIKLI EEQSINRLFL
PFVALQALAE AALSIEVFPS SLNEIMTAGE QLKITSQLKT FFTALDGCIL YNQYGPTECH
VVTQLKLEGD PEHWPALPNI GKPIDHTAIY ILNEHQHIEE NGVTGELCIT GSCLAEGYLG
NEELTKEKFS TLKISDATEI KMYRTGDVAR FLPDGNIEFL GREDEQVKIS GHRIELSEVE
IALNTLPNIT QAVVVASTHF SEQAQLIAYL KANGASEDSP KFRQQVNDAL PEYMLPSYFI
WVDEFPKTTS GKVAKKELPL PEYKRPTTAP LYKKPTTDTQ KNIAQVWSKI LRISKIGIWD
NFFEMGGTSL LAQKTVLTLR QQFKYEIPII KLYQHPTILE LSNFLAPKKS IQKKQNQRKQ
NYRSSSIAVI GMAGRFPGAN SIQELWEVLR DERETITFFT PEELDPSIPK ALVNDPLYVP
ARGIIPTAKE FDASFFGLNI KNAEVMDPQQ RLFLEIAWEV LEQTGHLTSH FDGKIGVYAG
TGMNTYYKNN ILPHKKVMDR VGSFLADTFN EKDYIASRTA YQLNLKGPAV SVHAACSTSS
LAIAQAVAAI RNGQCDVALA GGSSVTAPIH MGHLYQEGSI MSPDGHCRPF DENAKGTIFS
DGAGVLLLKR LEDAEQDGDT IHALIRGVGI NNDGGNKGSF TAPSTEGQAD AISLALFDAK
VNPSEISYVE THGTATPVGD PIEIEGLKMA FGEQEEHGFC AIGSIKSNMG HLTGAAGVSG
VIKTILALKN QQIPASLGFK KPNPSIDFEN SPFYVNNKLS PWNSKGLRKA GVSSFGVGGT
NVHIIVEEYE NKKIKSNAIR PLQLLMWSAK SAHSAIGYQK ALGEYIDPLS NMKLSDIAHS
LNRTRAEFAY RSFAIANTLV EAKEILSSDN HKQVKTNELK IDPSELAFLF PGQGSQYLQM
GKSLYKEEIV FKKAVDRCAK ILKNNLKLDI KDIIYPKDNS AQAAEKLKDT KFTQPALFVV
EYALAQLWMS WGIKPTLLCG HSIGEFVAAH LAGIFSLEDA LQLITMRGKL VSELPGGSML
SVRSTIDDIK NLIPNELSIA AINSDRLIVI SGPDNAIENF STVLHKKGIA NKLLLTSHAF
HSTMMDPVLD VFETEVKKVS LSLPRIPIVS TVTGTWLTDE EATSFTYWTN HLRAAVNFSG
AMETVLRLED TVLLEVGPGR ALSTLSMQKK GLKPLAAIAS LPLPKENKNA HHAVLAALGD
LWLTGITPDW ASFYGNQISK KVALPAYVFD RKPCWIAPVT VEREIKTIQT KQQINTARQP
QETNHNTKHT FMRKPVILKK ISEIVENNSG IEIEASEFKL SFLELGLDSL VLTQMAINLK
NEFNTPITFR QLNDDLESPD LLAEHLDKTL PKEFLAPASL AEPTTEHVQA TANHATSFNA
APQNLNTIAA PNQNTALGLI AQQIQLLGQQ IQLIQTSGNA GNQVIAKQPN TATEINTPAT
SPTPRSTAND MLSDDEKKEH QKPFGATPRI EKQTDNLSSS QKDFLENLII SYNKKTESSK
AYSQKHRHHM SDPRVVSGFK PLTKELVYPI VVDKSLGSRL WDIDGNEYLD VLNSFGACLF
GHQPNFIKEA IHKQVELGFE VGPQHPLAGE VCELLCEFTG QDRAALCNTG SEAVLGAMRI
ARTVTGRSLI VAFTTSYHGI NDEVIVRGSK KLKSFPAASG ILPEAVQNML ILDYGTDESL
AIIKERAHEI AAVLVEPVQS RRPDFRPIEF LKEVRKITTA SESVLIFDEI ITGFRTHPGG
AQSLFGIKAD IGTYGKVIGG GISIGAIIGN KKCMDALDGG HWQYGDDSFP EAGVTYFAGT
FVRHPLALAT CKASLLHMKE KGEALQDELA RKTEHFATEI NSYFELKNLP MKIMFYRSLW
KLKLEEEIPY AELFFVLMRE KGIHIWDGFP CYMTEAYTEE DLLHLINTSK ECINELISAG
FLKSEPSHRS NEKNQKSLTK ELNQPPVPGA RLGIDESGNP AWFIEDKDKT GQYVQIDL
//
