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Database: UniProt
Entry: Q5NN16_ZYMMO
LinkDB: Q5NN16_ZYMMO
Original site: Q5NN16_ZYMMO 
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
//
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