ID J2HJE5_9CAUL Unreviewed; 383 AA.
AC J2HJE5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|RuleBase:RU003693};
DE EC=2.3.1.47 {ECO:0000256|RuleBase:RU003693};
GN ORFNames=PMI01_01184 {ECO:0000313|EMBL:EJL35828.1};
OS Caulobacter sp. AP07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL35828.1, ECO:0000313|Proteomes:UP000007300};
RN [1] {ECO:0000313|EMBL:EJL35828.1, ECO:0000313|Proteomes:UP000007300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP07 {ECO:0000313|EMBL:EJL35828.1,
RC ECO:0000313|Proteomes:UP000007300};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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, ECO:0000256|RuleBase:RU003693}.
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 ECO:0000256|RuleBase:RU003693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604723-51, ECO:0000256|RuleBase:RU003693};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746, ECO:0000256|RuleBase:RU003693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU003693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily.
CC {ECO:0000256|ARBA:ARBA00010008, 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:EJL35828.1}.
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DR EMBL; AKKF01000083; EJL35828.1; -; Genomic_DNA.
DR RefSeq; WP_007665084.1; NZ_AKKF01000083.1.
DR AlphaFoldDB; J2HJE5; -.
DR PATRIC; fig|1144304.3.peg.1124; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000007300; Unassembled WGS sequence.
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:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR004723; AONS_Archaea/Proteobacteria.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00858; bioF; 1.
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|PIRSR:PIRSR604723-51};
KW Transferase {ECO:0000256|RuleBase:RU003693}.
FT DOMAIN 42..374
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604723-51"
SQ SEQUENCE 383 AA; 39820 MW; 16C4E611E2E2B4CC CRC64;
MHSLDTYAGD KLDRLEAASL LRRLKPTQRL AGAFVERDGR RLLSFSCNDY LGLAHHPKVK
AAAQAAIADH GAGAGASRLV TGDHPLLWQL EARLARLKGT QACVVFGSGY LANAGVIPTF
AGKGDIVLVD ELAHACIWAG AQLSGARIIP FAHNDTDHLA ALLAEHRASA RHALVATDGV
FSMDGDIAPL DWLSAVCEAN DAWLLSDDAH GVGVLADGRG SAALFPDAQI PFQMGTLSKA
LGSYGGYVCG SQAVVDLIKT RARTLVYTTG LPPAAAAAAL AALDVIEAEP ALTALPLAKA
QAFTKAVGLR PATSPIVPVI IGEAQAALDA SKALEAEGFL VVAIRPPTVP DGAARLRIAF
SAEHPDAEVA RLAALVRPYI KAR
//
