GenomeNet

Database: UniProt
Entry: A0A124FZL1_9FIRM
LinkDB: A0A124FZL1_9FIRM
Original site: A0A124FZL1_9FIRM 
ID   A0A124FZL1_9FIRM        Unreviewed;       257 AA.
AC   A0A124FZL1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:KUK84715.1};
DE   Flags: Fragment;
GN   ORFNames=XE00_0593 {ECO:0000313|EMBL:KUK84715.1};
OS   Desulfofundulus kuznetsovii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofundulus.
OX   NCBI_TaxID=58135 {ECO:0000313|EMBL:KUK84715.1, ECO:0000313|Proteomes:UP000054111};
RN   [1] {ECO:0000313|Proteomes:UP000054111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:KUK84715.1}.
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; LGGU01000019; KUK84715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124FZL1; -.
DR   PATRIC; fig|58135.3.peg.122; -.
DR   Proteomes; UP000054111; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; 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; 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   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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}.
FT   DOMAIN          37..257
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   NON_TER         257
FT                   /evidence="ECO:0000313|EMBL:KUK84715.1"
SQ   SEQUENCE   257 AA;  28078 MW;  3811DD8EF0222BAD CRC64;
     MEFLKTELDY LRNANLYRQL RWFEGSQSPR TTVNGRDCIL LSSNNYLGLT DHPDVKDAAL
     KALARWGTGS GGSRLISGNF FLYKELEDKI AQFKNAEEVI VFSSGYLTNI GTISSLVGPE
     DAVISDELNH ASIIDGCRLS RARVVIFGHK DMLQLEKALN ETQDCRRRLV ITDGVFSMDG
     DLAPLPEIVA LAEKNDAFVM VDDAHATGIL GSQGTGTVEH FNLEGKVAVQ VGTLSKALAS
     CGGYVTGKSD LINYLRN
//
DBGET integrated database retrieval system