BIKB_THET8
ID BIKB_THET8 Reviewed; 395 AA.
AC Q5SHZ8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase;
DE Short=AONS/AKB ligase;
DE EC=2.3.1.29;
DE EC=2.3.1.47;
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase;
DE Short=7-KAP synthase;
DE Short=KAPA synthase;
DE AltName: Full=8-amino-7-ketopelargonate synthase;
DE AltName: Full=Alpha-oxoamine synthase;
DE AltName: Full=Glycine acetyltransferase;
GN OrderedLocusNames=TTHA1582;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=18071260; DOI=10.1271/bbb.70438;
RA Kubota T., Shimono J., Kanameda C., Izumi Y.;
RT "The first thermophilic alpha-oxoamine synthase family enzyme that has
RT activities of 2-amino-3-ketobutyrate CoA ligase and 7-keto-8-
RT aminopelargonic acid synthase: cloning and overexpression of the gene from
RT an extreme thermophile, Thermus thermophilus, and characterization of its
RT gene product.";
RL Biosci. Biotechnol. Biochem. 71:3033-3040(2007).
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 (By similarity). Can also
CC use pimeloyl-CoA instead of pimeloyl-ACP as substrate. It also converts
CC 2-amino-3-ketobutyrate and CoA to glycine and acetyl-CoA. Activity is
CC also observed with the following combinations of substrates: acetyl-CoA
CC and either L-alanine or L-serine, pimeloyl-CoA and either glycine or L-
CC serine, and palmitoyl-CoA with L-alanine. {ECO:0000250,
CC ECO:0000269|PubMed:18071260}.
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:0000269|PubMed:18071260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA;
CC Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29;
CC Evidence={ECO:0000269|PubMed:18071260};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 uM for L-glycine (with acetyl-CoA at pH 6 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:18071260};
CC KM=11.8 uM for L-alanine (with pimeloyl-CoA at pH 6 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:18071260};
CC KM=30 uM for acetyl-CoA (with L-glycine at pH 6 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:18071260};
CC KM=80 uM for pimeloyl-CoA (with L-alanine at pH 6 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:18071260};
CC pH dependence:
CC Optimum pH is 6.0. Stable at pH 4.5-5.0, and a loss of less than 10%
CC of the initial activity is observed after 1 hour of incubation at
CC these pH. {ECO:0000269|PubMed:18071260};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Stable at temperatures up
CC to 70 degrees Celsius, with a loss of less than 10% of the initial
CC activity observed after 1 hour of incubation at these temperatures.
CC The enzyme shows a half-life of 1 hour at 80 degrees Celsius.
CC {ECO:0000269|PubMed:18071260};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18071260}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AP008226; BAD71405.1; -; Genomic_DNA.
DR RefSeq; WP_011228785.1; NC_006461.1.
DR RefSeq; YP_144848.1; NC_006461.1.
DR AlphaFoldDB; Q5SHZ8; -.
DR SMR; Q5SHZ8; -.
DR STRING; 300852.55772964; -.
DR EnsemblBacteria; BAD71405; BAD71405; BAD71405.
DR GeneID; 3169187; -.
DR KEGG; ttj:TTHA1582; -.
DR PATRIC; fig|300852.9.peg.1553; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_0; -.
DR OMA; MDTHGFG; -.
DR PhylomeDB; Q5SHZ8; -.
DR SABIO-RK; Q5SHZ8; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IDA:UniProtKB.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR010962; AONS_Archaea/Firmicutes.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00858; bioF; 1.
DR TIGRFAMs; TIGR01825; gly_Cac_T_rel; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="8-amino-7-oxononanoate synthase/2-amino-3-
FT ketobutyrate coenzyme A ligase"
FT /id="PRO_0000381125"
FT BINDING 110..111
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 207..210
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 239..242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 43362 MW; AD5D070211FAA581 CRC64;
MSLDLRARVR EELERLKREG LYISPKVLEA PQEPVTRVEG REVVNLASNN YLGFANHPYL
KEKARQYLEK WGAGSGAVRT IAGTFTYHVE LEEALARFKG TESALVLQSG FTANQGVLGA
LLKEGDVVFS DELNHASIID GLRLTKATRL VFRHADVAHL EELLKAHDTD GLKLIVTDGV
FSMDGDIAPL DKIVPLAKKY KAVVYVDDAH GSGVLGEKGK GTVHHFGFHQ DPDVVQVATL
SKAWAGIGGY AAGARELKDL LINKARPFLF STSHPPAVVG ALLGALELIE KEPERVERLW
ENTRYFKREL ARLGYDTLGS QTPITPVLFG EAPLAFEASR LLLEEGVFAV GIGFPTVPRG
KARIRNIVTA AHTKEMLDKA LEAYEKVGKR LGIIR
