ID A0A1H8GZF2_9ACTN Unreviewed; 1267 AA.
AC A0A1H8GZF2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
GN ORFNames=SAMN05660976_07689 {ECO:0000313|EMBL:SEN48877.1};
OS Nonomuraea pusilla.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46177 {ECO:0000313|EMBL:SEN48877.1, ECO:0000313|Proteomes:UP000198953};
RN [1] {ECO:0000313|EMBL:SEN48877.1, ECO:0000313|Proteomes:UP000198953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43357 {ECO:0000313|EMBL:SEN48877.1,
RC ECO:0000313|Proteomes:UP000198953};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-
CC oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846,
CC ChEBI:CHEBI:149468; EC=2.3.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00034067};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; FOBF01000027; SEN48877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8GZF2; -.
DR STRING; 46177.SAMN05660976_07689; -.
DR OrthoDB; 9807157at2; -.
DR Proteomes; UP000198953; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd06454; KBL_like; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693:SF3; LD36009P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198953};
KW Transferase {ECO:0000313|EMBL:SEN48877.1}.
FT DOMAIN 689..763
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 437..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 133741 MW; 4B270A35956B9FB7 CRC64;
MSGIRLHLRA ADPLVADHRI GDTPVIAAAT QIDAVLRACD ARRPDSVWTL EHVAFRAPLR
VTGPDVEIEV VTAEDGQCSV RSAGVEYGSA RTRGEPLPPP RYLDVTALRA GCERDVPLTD
VAAWRRASGI TYGPAFQAIR TAYAGPGRML AVLRATDDLH APAFVPPPLL DGVFQCLGML
DTGAAQAFLP WHVGRIVARR RITGTVLALV ERDTAQGAAG AALRGRATVC NQQGEVLLEL
ERITLKAASF RAPQPPPAAT PPLVQTVTWR RTDPAAAPSA PGSASAPSAL DGPVLLVSEH
DVAAPPGRLT VRLTPGELTV ERLDETLAGG PVQEVVYVAP EGVASPKQVT AALQGAFTLV
RRLAARPPMP DLLIVTAGAH DVTGGEPVDP FMTALWGLGR TLRLEHPRTT VRLVDLEPGG
AAPPWDAPRA ELELARRGGS WHAPSLEPHP PATGAPPRFR GGRFLITGGM GAIGLRVAEF
LAEEGCAHLT LVGRTVPDGG ETRRRLDRLG ALCELDVVAA DVRFLPGVLG GAARYDGVFH
TAGVLRDGLA RSLTPRQVEE VLDPKVGGVH ALAELVAGHA PPGFVALFSS ISAVRANLGQ
SSYAAANAYL DGYAARRRAA GEPWYSLGWG LWAIGMGEDV APKAAAHGIP ALTADDGVAL
LRAVLSRPPA NYVLSAAAHA KGEPMTAVTP ESGLWPQLTA AVKKILHVDD VMPEDDLLEL
GLDSMMAVEL AASLSGGGLD VDPMVFFEHS RVGVLLGRLE SLPRTGAAGG PAAGEPRETP
PPVPRDERPA PAPEGRAAGS FVSPWDRYRE PASARPVESP PSRVPPKPAP PVPIIPTVPT
VPAAPPPSAA PRANGRVPRR TLPGRLSNAA DGTFLDRRID ALSEEDRLIV ARDEYFYEPV
IEQAEGARIK FDGRWFLNFA SYSYLGLIGH DYIDQQVLDA VERHGTGAHG VRLLAGTLHL
HRELELSLAR FLGAEDAVVY SSGYMANVAT VSALVGPGDV IVGDVYNHAS ILDGYRLSGA
DVITYAHNDL ADLERALKKV GDAGRLVVTD AVFSMDGDVA DLPGILELCE RYDAPLMVDE
AHSLGVLGDT GRGITEHFGI DPARVDVKMG TLSKTVPSAG GYVAGSRDLI FALKNNARGW
MFSAAATPAQ VAAAKAAIEV MAAAPELTRE LRARTARYHE RLRALGFDTL ASETPVVPII
CRSAGQAGAM ARLCQLDGLF VQPIVYPAVP RTLPRLRTIV NLSHSEADLD TAVATLEKAG
RACGLIS
//
