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Database: UniProt
Entry: B0SZZ7_CAUSK
LinkDB: B0SZZ7_CAUSK
Original site: B0SZZ7_CAUSK 
ID   B0SZZ7_CAUSK            Unreviewed;       400 AA.
AC   B0SZZ7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Aminotransferase class I and II {ECO:0000313|EMBL:ABZ72070.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Caul_2943 {ECO:0000313|EMBL:ABZ72070.1};
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ72070.1};
RN   [1] {ECO:0000313|EMBL:ABZ72070.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31 {ECO:0000313|EMBL:ABZ72070.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC       carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC       [acyl-carrier protein], and carbon dioxide.
CC       {ECO:0000256|ARBA:ARBA00002513}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP000927; ABZ72070.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0SZZ7; -.
DR   STRING; 366602.Caul_2943; -.
DR   KEGG; cak:Caul_2943; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_2_5; -.
DR   OrthoDB; 9807157at2; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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: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.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:ABZ72070.1};
KW   Transferase {ECO:0000313|EMBL:ABZ72070.1}.
FT   DOMAIN          50..381
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   400 AA;  42570 MW;  9D1370DF6F4D15DD CRC64;
     MIAPDPCAGS AEPTYPAWLH RHLDEQAAII RALDPFPFAQ PADTTGFHSL HQNDYLRLSN
     HPEVIRARTE AASRSRVDSF SSFVFGGAAA EHETFAALLR EALQACQVIA TTAGWTANVG
     LIEAIAAPDV PIYVDAEAHA SLLDGVRLSL GRRLLFRHND PQHLEDRIAI HGPGIVIIDA
     LYSTDGTLAD LPRFVAICER HECTLILDEA HSFGMFGEAG GGLAVACGLA HRVHFRTLSL
     SKALGGHGGA IACGAQIAPA LWSRLRPVIF SSATSSILAA AHAKALELTM TDRRRAEHCQ
     AMATLLRDRL NASGIDTLGS ASQIISIKLQ GGDAAKLYGA LRERGVLTSV FIYPAVQMGI
     SLVRLSVHAE VTEADVDYVS ATIVESLEAL GLGMDGRVAA
//
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