BIOA_HAEIN
ID BIOA_HAEIN Reviewed; 430 AA.
AC P44426;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
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}; OrderedLocusNames=HI_1554;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
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; L42023; AAC23203.1; -; Genomic_DNA.
DR PIR; E64129; E64129.
DR RefSeq; NP_439703.1; NC_000907.1.
DR RefSeq; WP_005693582.1; NC_000907.1.
DR AlphaFoldDB; P44426; -.
DR SMR; P44426; -.
DR STRING; 71421.HI_1554; -.
DR EnsemblBacteria; AAC23203; AAC23203; HI_1554.
DR KEGG; hin:HI_1554; -.
DR PATRIC; fig|71421.8.peg.1625; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_6; -.
DR OMA; VAVKMCL; -.
DR PhylomeDB; P44426; -.
DR BioCyc; HINF71421:G1GJ1-1574-MON; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..430
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120369"
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 147
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 430 AA; 47606 MW; 0E391250BC3B0602 CRC64;
MVDEQSLLAF DTQHIWHPYS SVSSDMPLYA VERADGVMIT LKDGRRLIDG MSSWWAALHG
YNHPRLNAAA QNQLAKMSHI MFGGFTHDPA VELAQLLVQI LPNGLDKIFF ADSGSVAVEV
AMKMAIQYQH AKGEVQRQKF ATIRSGYHGD TWNAMSVCDP TTGMHHLFHH SLPVQYFLPQ
PNIPFNESWN DCAIEPLADL LKKKGNEIAA LILEPVVQGA GGMYFYSPTY LVKAQALCKQ
YGILLIFDEI ATGFGRTGKL FAAEHAGISP DIMCIGKALT GGYLTLSASI TTTEIAQTIC
SGEAKCFMHG PTFMANPLAC AIAAESIRLL LESPWQQNIQ RIESSLKQQL SPLSEKDYVK
EVRALGAIGV VEMKSAVNMK TLVPRFVEQG VWIRPFGKLV YVMPPFVIKD DELQKLTEGM
ILALTQEYEH
