GenomeNet

Database: UniProt
Entry: A0A0M3T5J3_9MICC
LinkDB: A0A0M3T5J3_9MICC
Original site: A0A0M3T5J3_9MICC 
ID   A0A0M3T5J3_9MICC        Unreviewed;       374 AA.
AC   A0A0M3T5J3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE            EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
DE   AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000256|ARBA:ARBA00032610};
DE   AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|ARBA:ARBA00033381};
GN   ORFNames=AL755_17510 {ECO:0000313|EMBL:ALE07955.1};
OS   Arthrobacter sp. ERGS1:01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE07955.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE07955.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE07955.1,
RC   ECO:0000313|Proteomes:UP000060433};
RX   PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT   bacterium with prospective cold active industrial enzymes, isolated from
RT   East Rathong glacier in India.";
RL   J. Biotechnol. 214:139-140(2015).
RN   [2] {ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
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         ECO:0000256|RuleBase:RU003693};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. BioF subfamily.
CC       {ECO:0000256|ARBA:ARBA00010008}.
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; CP012479; ALE07955.1; -; Genomic_DNA.
DR   RefSeq; WP_054013167.1; NZ_CP012479.1.
DR   AlphaFoldDB; A0A0M3T5J3; -.
DR   STRING; 1704044.AL755_17510; -.
DR   KEGG; are:AL755_17510; -.
DR   PATRIC; fig|1704044.3.peg.2842; -.
DR   OrthoDB; 9807157at2; -.
DR   Proteomes; UP000060433; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-KW.
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:SF100; 8-AMINO-7-OXONONANOATE SYNTHASE; 1.
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   Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060433}.
FT   DOMAIN          27..360
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   374 AA;  37804 MW;  31A4C1768DB2FD83 CRC64;
     MDSWLRSRAA VRVRRGLVRR TEPQAGLIDL ASNDYLGLAG DPRLAAAAAR ATDEHGTGAR
     ASRVVCGTTG AHQGLERALC RLTGQDAALA FSSGYTANLG VLTALGGPGT LFIYDAHVHA
     SLLDGIRLSR SEAVEVPHND LAAVATALAA RGQPRAVVVL ESIYSVLGDA APLAEAAALC
     AEFDALLLVD EAHGIGVAGD GRGAVHAAGL AGTRHVAVTA TLSKALGSQG GAVLGSTLLR
     EHLVNTARTF IFDTALAPAA AAAAAEAAGI VLAEPELAHR VLRNAQVLAL ACGTEPSAGA
     VQSIPVGSPE RAATVTAALR AAGVAVGCFR PPSVPDGVSR VRLTARANLT DAELRRAAAS
     VNRALESGLQ EVPA
//
DBGET integrated database retrieval system