ID A0A0N1FXU2_9ACTN Unreviewed; 452 AA.
AC A0A0N1FXU2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
GN ORFNames=OK074_4188 {ECO:0000313|EMBL:KPI06210.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI06210.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI06210.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI06210.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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};
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:KPI06210.1}.
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DR EMBL; LJCV01000258; KPI06210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1FXU2; -.
DR PATRIC; fig|1592327.3.peg.6566; -.
DR OrthoDB; 9807157at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KPI06210.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transferase {ECO:0000313|EMBL:KPI06210.1}.
FT DOMAIN 94..438
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 47681 MW; FF68116FB10B77AC CRC64;
MTTTVPAPAP APAPTPTAGP LGGDRRTDAL EKDIMRFRTV SGPDLTTRND AYLAWQLDRQ
QADLWPYFRH YETPALTTRA TVVSDTGVVT DGPNFGGQDY LSLTSHPAVR DAAHQALRDY
GPLTAGSPAL GGATPISRAL EAGLAEALRT EHVALFPTGW ASGFGTIRAL MHRRDHILLD
KLSHDSLRQG AAASGATVEF FRHLDNDAVR RHLSGIRAND TKNAVLVVTE GVFSMDSDTP
HLAELLGVCR EFGAQLMVDV AHDFGAMGEH GGGQPEVHGI LGEVDFVVGA FSKTFATTGG
FLATPSASAR EFVRMFGGPQ TFSSAITPVQ TAVALAALGV VTSPEGARRR AAVAAVATRL
RAGLTARGLE VMGDVVCPVV PVLIGDTPTG RTASGLIARA GLVAHLVEQP AVASDAARFR
MQAMADHTDD DVDTAIDILD TCIREARRTT AR
//
