ID D9SJ14_GALCS Unreviewed; 384 AA.
AC D9SJ14;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE Short=AONS {ECO:0000256|HAMAP-Rule:MF_01693};
DE EC=2.3.1.47 {ECO:0000256|HAMAP-Rule:MF_01693};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE Short=7-KAP synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE Short=KAPA synthase {ECO:0000256|HAMAP-Rule:MF_01693};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|HAMAP-Rule:MF_01693};
GN Name=bioF {ECO:0000256|HAMAP-Rule:MF_01693};
GN OrderedLocusNames=Galf_0245 {ECO:0000313|EMBL:ADL54290.1};
OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS capsiferriformans (strain ES-2)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Gallionella.
OX NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL54290.1, ECO:0000313|Proteomes:UP000001235};
RN [1] {ECO:0000313|EMBL:ADL54290.1, ECO:0000313|Proteomes:UP000001235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-2 {ECO:0000313|EMBL:ADL54290.1,
RC ECO:0000313|Proteomes:UP000001235};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA Woyke T.;
RT "Complete sequence of Gallionella capsiferriformans ES-2.";
RL Submitted (AUG-2010) 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. {ECO:0000256|HAMAP-
CC Rule:MF_01693}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01693, ECO:0000256|PIRSR:PIRSR604723-51};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746, ECO:0000256|HAMAP-Rule:MF_01693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01693}.
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DR EMBL; CP002159; ADL54290.1; -; Genomic_DNA.
DR RefSeq; WP_013292233.1; NC_014394.1.
DR AlphaFoldDB; D9SJ14; -.
DR STRING; 395494.Galf_0245; -.
DR KEGG; gca:Galf_0245; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_4; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001235; Chromosome.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06454; KBL_like; 1.
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 HAMAP; MF_01693; BioF_aminotrans_2; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004723; AONS_Archaea/Proteobacteria.
DR InterPro; IPR022834; AONS_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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ADL54290.1};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW Rule:MF_01693};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01693,
KW ECO:0000256|PIRSR:PIRSR604723-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000001235};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01693, ECO:0000313|EMBL:ADL54290.1}.
FT DOMAIN 40..379
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 107..108
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 178
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 206
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693"
FT MOD_RES 237
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01693,
FT ECO:0000256|PIRSR:PIRSR604723-51"
SQ SEQUENCE 384 AA; 41140 MW; 2DF46C7E43D6798C CRC64;
MPFTELQLEL DERCARGLLR QRRTVSSPQT PELVVEGKPY LSFSSNDYLG LANHPDIISA
LQQGAAEYGV GAGAAHLVCG HFTPHEQLEC ELAAFAGKPA ALLFSTGYMA NLGVVQGLVG
RGDTVFADKL NHASLNDAML LSRATVQRYR HNDMAQLAVL LAQTGRGRKL ICVDAVFSMD
GDMAPLPELL ALCVAHDAWL LVDDAHGFGV LGHQGRGSLS HFGLSSPRII YMATLGKAAG
VSGAFVAAEQ AVIDTLINNA HSYVYTTASP PALACALRQS LQLIAEEDRR RAHLHQLIAQ
LRTGLHGLPW QLMPSDTAIQ PLLVGDNQAA LALSMALRAR GIWVAAIRPP TVPAGTARLR
ITLSAAHTED DVSRLLEALH ELAR
//
