ID Q5NN16_ZYMMO Unreviewed; 403 AA.
AC Q5NN16;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:AAV89894.1};
DE EC=2.3.1.47 {ECO:0000313|EMBL:AAV89894.1};
GN OrderedLocusNames=ZMO1270 {ECO:0000313|EMBL:AAV89894.1};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV89894.1, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV89894.1, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR EMBL; AE008692; AAV89894.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5NN16; -.
DR STRING; 264203.ZMO1270; -.
DR KEGG; zmo:ZMO1270; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_5; -.
DR OMA; RSQMFAK; -.
DR Proteomes; UP000001173; Chromosome.
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 CDD; cd06454; KBL_like; 1.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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 PANTHER; PTHR13693:SF3; LD36009P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AAV89894.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000001173};
KW Transferase {ECO:0000313|EMBL:AAV89894.1}.
FT DOMAIN 48..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 43785 MW; 35EAD44276FAF67A CRC64;
MQVTDLFSKF DPLIAIRKEM LSHGGRDPFA VVMEKVLSPT KAIIKGKPVI LLGTYNYMGM
TFDPDVIAAG EKALKEFGAG TTGSRVLNGT YQGHKACEEA LKDYYGMEHA MVFSTGYQAN
LGMISTLAGK GEYVIIDADS HASIYDGCRL GNAEIIRFRH NSPEDLDRRL ARLPKEAGKL
VVLEGVYSML GDIAPLAEMV AIAKKHDALI LDDEAHGMGF FGKNGRGVFE ELGLEGQIDF
IVGTFSKSVG TVGGFCVSNH PQFEVLRLVC RPYVFTASLP PSVVATAEAS IRKLQKANDK
REHLWKNSRR LHGGLKEMGF KLGTETAQSA IIAVILPDQE QAVAMWQNLL ELGLYVNLAR
PPATPAGMFL LRCSLCAEHS DDDVTEILAM FKKAGQATGV LAA
//