BIOA_SYNE7
ID BIOA_SYNE7 Reviewed; 424 AA.
AC Q31SA6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE EC=2.6.1.62 {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DAPA AT {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DAPA aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DANS {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00834};
GN Name=bioA {ECO:0000255|HAMAP-Rule:MF_00834, ECO:0000303|PubMed:32042199};
GN OrderedLocusNames=Synpcc7942_0031;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=32042199; DOI=10.1038/s41589-019-0461-9;
RA Sakaki K., Ohishi K., Shimizu T., Kobayashi I., Mori N., Matsuda K.,
RA Tomita T., Watanabe H., Tanaka K., Kuzuyama T., Nishiyama M.;
RT "A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in
RT cyanobacteria.";
RL Nat. Chem. Biol. 16:415-422(2020).
CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to
CC form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase
CC known to utilize SAM as an amino donor (By similarity). Complements a
CC bioU deletion in Synechocystis PCC 6803 (PubMed:32042199).
CC {ECO:0000255|HAMAP-Rule:MF_00834, ECO:0000269|PubMed:32042199}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine =
CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-
CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469;
CC EC=2.6.1.62; Evidence={ECO:0000255|HAMAP-Rule:MF_00834};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00834};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00834}.
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DR EMBL; CP000100; ABB56063.1; -; Genomic_DNA.
DR RefSeq; WP_011243776.1; NC_007604.1.
DR AlphaFoldDB; Q31SA6; -.
DR SMR; Q31SA6; -.
DR STRING; 1140.Synpcc7942_0031; -.
DR PRIDE; Q31SA6; -.
DR EnsemblBacteria; ABB56063; ABB56063; Synpcc7942_0031.
DR KEGG; syf:Synpcc7942_0031; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_3; -.
DR OMA; VAVKMCL; -.
DR OrthoDB; 478143at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0031-MON; -.
DR UniPathway; UPA00078; UER00160.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase 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; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Biotin biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..424
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000450577"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 106..107
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 240
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 304..305
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT SITE 11
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT MOD_RES 269
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
SQ SEQUENCE 424 AA; 45867 MW; 65E4829A23539F5B CRC64;
MPSHPHLWFP FTSVKDAPDP LKVVSGKGAR LTLADGRELI DCISSWWVNL HGHAHLRIVE
AIAQQAATLE HVIFAGFSHE PAERLAMELC KILPEKLTRV FFSDNGSTAV EVALKMALQY
WHNLDQPRSR ILAFDGAYHG DTFGAMSVGE RSLFNAPFEK LLFSVEFLPY PETWWGDETV
EAKEAAAIAA VEQALAAGDV AAVIIEPLVQ GAGGMRMARP QFLQQLAARV QAAGSLLIAD
EVMTGFGRTG AWFACQRAGI QPDLICLSKG LTGGFLPLSI TVATEVIYDT FCSGNPDHTF
YHGHSYTANP LGCAAAIASL ELLLDSEAIV QGLEDAHLPG LELLAQHPKV TRPRLTGGIA
ACDLVSDRGG YLDPIGLRVR QAAIARGLLL RPLGNVLYLL PPYCLTPTEL QDIYAAIADL
LDEI
