BIOA_MYCBO
ID BIOA_MYCBO Reviewed; 437 AA.
AC P0A4X7; A0A1R3XYQ6; O06622; X2BIJ6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
GN OrderedLocusNames=BQ2027_MB1595;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG / Pasteur;
RA Yu S., Jacobs W.R. Jr.;
RT "Cloning, sequencing, and identification of Mycobacterium bovis BCG biotin
RT biosynthetic genes by complementing two Mycobacterium smegmatis biotin
RT mutants.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; AF041819; AAB96956.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU00198.1; -; Genomic_DNA.
DR RefSeq; NP_855247.1; NC_002945.3.
DR RefSeq; WP_003407803.1; NC_002945.4.
DR PDB; 5KGS; X-ray; 2.10 A; A/B=1-437.
DR PDB; 5KGT; X-ray; 2.25 A; A/B=1-437.
DR PDB; 5TE2; X-ray; 1.80 A; A/B=1-437.
DR PDBsum; 5KGS; -.
DR PDBsum; 5KGT; -.
DR PDBsum; 5TE2; -.
DR AlphaFoldDB; P0A4X7; -.
DR SMR; P0A4X7; -.
DR EnsemblBacteria; SIU00198; SIU00198; BQ2027_MB1595.
DR GeneID; 45425552; -.
DR PATRIC; fig|233413.5.peg.1742; -.
DR OMA; VAVKMCL; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000001419; Chromosome.
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 3D-structure; Aminotransferase; Biotin biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..437
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120372"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 124..125
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 254
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 317..318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT SITE 25
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 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:5TE2"
FT TURN 170..174
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5TE2"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:5TE2"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:5TE2"
FT TURN 256..263
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5TE2"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:5TE2"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:5KGS"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:5TE2"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:5TE2"
FT HELIX 416..433
FT /evidence="ECO:0007829|PDB:5TE2"
SQ SEQUENCE 437 AA; 46319 MW; 8E6B6EDE4F0AE7F6 CRC64;
MAAATGGLTP EQIIAVDGAH LWHPYSSIGR EAVSPVVAVA AHGAWLTLIR DGQPIEVLDA
MSSWWTAIHG HGHPALDQAL TTQLRVMNHV MFGGLTHEPA ARLAKLLVDI TPAGLDTVFF
SDSGSVSVEV AAKMALQYWR GRGLPGKRRL MTWRGGYHGD TFLAMSICDP HGGMHSLWTD
VLAAQVFAPQ VPRDYDPAYS AAFEAQLAQH AGELAAVVVE PVVQGAGGMR FHDPRYLHDL
RDICRRYEVL LIFDEIATGF GRTGALFAAD HAGVSPDIMC VGKALTGGYL SLAATLCTAD
VAHTISAGAA GALMHGPTFM ANPLACAVSV ASVELLLGQD WRTRITELAA GLTAGLDTAR
ALPAVTDVRV CGAIGVIECD RPVDLAVATP AALDRGVWLR PFRNLVYAMP PYICTPAEIT
QITSAMVEVA RLVGSLP
