BIOF_PARP8
ID BIOF_PARP8 Reviewed; 394 AA.
AC B2JKH6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=AONS {ECO:0000255|HAMAP-Rule:MF_01693};
DE EC=2.3.1.47 {ECO:0000255|HAMAP-Rule:MF_01693};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=7-KAP synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE Short=KAPA synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
GN Name=bioF {ECO:0000255|HAMAP-Rule:MF_01693}; OrderedLocusNames=Bphy_0172;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01693};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01693}.
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DR EMBL; CP001043; ACC69365.1; -; Genomic_DNA.
DR RefSeq; WP_012399594.1; NZ_CADFGH010000001.1.
DR PDB; 6ONN; X-ray; 1.80 A; A/B=1-394.
DR PDBsum; 6ONN; -.
DR AlphaFoldDB; B2JKH6; -.
DR SMR; B2JKH6; -.
DR STRING; 391038.Bphy_0172; -.
DR EnsemblBacteria; ACC69365; ACC69365; Bphy_0172.
DR KEGG; bph:Bphy_0172; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_4; -.
DR OMA; HYHASGI; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001192; Chromosome 1.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00858; bioF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..394
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000380941"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 211
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT HELIX 2..17
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:6ONN"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:6ONN"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 292..314
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 334..346
FT /evidence="ECO:0007829|PDB:6ONN"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6ONN"
FT HELIX 376..393
FT /evidence="ECO:0007829|PDB:6ONN"
SQ SEQUENCE 394 AA; 41743 MW; 136C7626B92FAAE0 CRC64;
MQLLDTLEQG LKEIDARGLR RRRRTVDSPC SAHMTVDGRN MIGFASNDYL GLAAHPLLVA
AITEGARRYG AGSGGSHLLG GHSRAHAQLE DDLAEFAGGF VDNPRALYFS TGYMANLATL
TALAGRGTTL FSDSLNHASL IDGARLSRAD IQIYPHADAE ALGAMLEASD AAVKLIVSDT
VFSMDGDIAP LARLLELAEH HGAWLVVDDA HGFGVLGPQG RGAVAEAALR SPHLIVVGTL
GKAAGVSGAF VVAHETVIEW LVQRARPYIF TTASVPSAAH AVSASLRIIG GDEGEHRRAH
LRSLIALTRD MLKSTPWLPV DSHTAVQPLI IGSNEATLDV AASLDRANLW VPAIRPPTVP
EGTSRLRISL SAAHSHNDLE QLEHALMKTA EARA
