BIOA_SERMA
ID BIOA_SERMA Reviewed; 425 AA.
AC P36568;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 99.
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};
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Sr41 / TLr156;
RX PubMed=8250549; DOI=10.1128/aem.59.10.3225-3232.1993;
RA Sakurai N., Imai Y., Masuda M., Komatsubara S., Tosa T.;
RT "Molecular breeding of a biotin-hyperproducing Serratia marcescens
RT strain.";
RL Appl. Environ. Microbiol. 59:3225-3232(1993).
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:0000255|HAMAP-
CC Rule:MF_00834, ECO:0000269|PubMed:8250549}.
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; D17468; BAA04284.1; -; Genomic_DNA.
DR AlphaFoldDB; P36568; -.
DR SMR; P36568; -.
DR STRING; 273526.SMDB11_0559; -.
DR PRIDE; P36568; -.
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..425
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120376"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 114..115
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 248
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 311..312
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT SITE 19
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 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
SQ SEQUENCE 425 AA; 46867 MW; 8BA657E59BB94AF6 CRC64;
MSVTASDLAF DQRHIWHPYT SMSRPLPCYP IESASGVELQ LADGRSLVDG MSSWWAAIHG
YNHPRLNQAA SQQLEKMSHV MFGGITHPAA ISLCRRLVEM TPEALQCVFL ADSGSVAVEV
SLKMALQYWQ ARGERRQRIL TLRHGYHGDT FGAMSVCDPD NSMHSLYQGY LAPHLFATAP
QCRFDEEWRE EDIAPFAALL EQHAGEVAAV ILEPVVQGAG GMRIYHPTYL KRVRDVVRVA
IKLLLIADEI ATGFGRTGKL FACEHAQVVP DILCLGKALT GGYMTLSATL TTRHVAETIS
NGAAGCFMHG PTFMGNPLAC AVADASLALL AENRWQAQVS AIETQLKREL LPLGRCRRWP
HVRVLGAIGV VEMREPVDVA ELQRGFVERG VWIRPFGKLI YLMPPYIIEA EQLSRLTAAV
ADAAR
