ID BIOA_METJA Reviewed; 461 AA.
AC Q58696;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 134.
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=MJ1300;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99307.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99307.1; ALT_INIT; Genomic_DNA.
DR PIR; C64462; C64462.
DR RefSeq; WP_064496781.1; NC_000909.1.
DR PDB; 6ZHK; X-ray; 1.80 A; A/B=1-461.
DR PDBsum; 6ZHK; -.
DR AlphaFoldDB; Q58696; -.
DR SMR; Q58696; -.
DR STRING; 243232.MJ_1300; -.
DR PaxDb; 243232-MJ_1300; -.
DR EnsemblBacteria; AAB99307; AAB99307; MJ_1300.
DR GeneID; 1452202; -.
DR KEGG; mja:MJ_1300; -.
DR eggNOG; arCOG00917; Archaea.
DR HOGENOM; CLU_016922_4_3_2; -.
DR InParanoid; Q58696; -.
DR OrthoDB; 6534at2157; -.
DR PhylomeDB; Q58696; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000000805; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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 NCBIfam; TIGR00508; bioA; 1.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..461
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120377"
FT BINDING 117..118
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 263
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
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:0000255|HAMAP-Rule:MF_00834"
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 117..135
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:6ZHK"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6ZHK"
FT TURN 265..272
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6ZHK"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6ZHK"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:6ZHK"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6ZHK"
FT HELIX 442..458
FT /evidence="ECO:0007829|PDB:6ZHK"
SQ SEQUENCE 461 AA; 52314 MW; 8CF29B3FCBC280FC CRC64;
MNIDKNLLEK WDKEYIWHPY TQMKEYRESK NLIIERGEGN YLIDIYGNKY LDAVSSIWCN
LFGHSRKEII EAIKNQADKI CHSTLLGCGN VPSILLAKKL VDITPKHLTK VFYSEDGAEA
VEIAIKMAYQ YYVLRGDKGR TKFISVKEGY HGDTVGAMSV GGSELFHGVF KPLLFKGYHA
NPPYCYRCKY HNFKDTDERN EKGCEMECLN EMISLIEKHA EEVFCVILEG GIMGSAGMIP
YPDGYIEGVA KACKENDVIF ILDEVATGFG RTGKMFFCDN EELKKLEKPD ILCLGKGLTG
GYLPLAATLT TDEIYNQFLG EFGESKQLYH GHTYTGNQLL CSAALATLEI FEKENVIENI
QPKIKLFHKE LRKLKELEHV GDVRGRGFMV GIELVKDKET KEPYPYGYKA GYRVAEKLLE
KGIYMRPIGN VIILVPPLSI TEKEIIYLCD ALYEAIKEAD L
//
