BIOA_LYSSH
ID BIOA_LYSSH Reviewed; 455 AA.
AC P22805;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
DE EC=2.6.1.62;
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase;
DE Short=DAPA AT;
DE Short=DAPA aminotransferase;
DE AltName: Full=7,8-diaminononanoate synthase;
DE Short=DANS;
DE AltName: Full=Diaminopelargonic acid synthase;
GN Name=bioA;
OS Lysinibacillus sphaericus (Bacillus sphaericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RX PubMed=2110099; DOI=10.1016/0378-1119(90)90496-e;
RA Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M.,
RA Villeval D., Kisou T., Kamogawa K., Lemoine Y.;
RT "Cloning and characterization of the Bacillus sphaericus genes controlling
RT the bioconversion of pimelate into dethiobiotin.";
RL Gene 87:63-70(1990).
RN [2]
RP FUNCTION AS A DAPA AMINOTRANSFERASE, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RA Izumi Y., Kano Y., Inagaki K., Kawase N., Tani Y., Yamada H.;
RT "Characterization of biotin biosynthetic enzymes of Bacillus sphaericus: a
RT dethiobion producing bacterium.";
RL Agric. Biol. Chem. 45:1983-1989(1981).
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. {ECO:0000269|Ref.2}.
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:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by KAPA at concentrations higher than
CC 0.05 mM. {ECO:0000269|Ref.2}.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000305}.
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DR EMBL; M29292; AAB02325.1; -; Genomic_DNA.
DR PIR; JQ0507; JQ0507.
DR AlphaFoldDB; P22805; -.
DR SMR; P22805; -.
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 1: Evidence at protein level;
KW Aminotransferase; Biotin biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..455
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120360"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117..118
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 20
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000250"
FT MOD_RES 285
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 51774 MW; A5298A500869855E CRC64;
MKQVLTELQE KDLQHVWHPC SQMKDYEAFP PIVIKKGEGV WLYDEQNQRY LDAVSSWWVN
LFGHANPRIS QALSEQAFTL EHTIFANFSH EPAIKLAQKL VALTPQSLQK VFFADNGSSA
IEVALKMSFQ YHMQTGKTQK KRFLALTDAY HGETLGALSV GGVDLYNEVY QPLLLDTVRA
QGPDCFRCPF KHHPDSCHAQ CISFVEDQLR MHHKEITAVI IEPLIQAAAG MKMYPAIYLR
RLRELCTQYD VHLIADEIAV GFGRTGTLFA CEQANISPDF MCLSKGLTGG YLPLSVVMTT
NDVYQAFYDD YATMKAFLHS HSYTGNTLAC RVALEVLAIF EEEQYIDVVQ DKGERMRKLA
LEAFSDLPFV GEYRQVGFVG AIELVANRDT KEPLPSEERI GYQIYKRALA KGLLIRPLGN
VLYFMPPYII TDDEMQFMIQ TTKDTIVQFF EEREG
