ID A0A244E767_9BURK Unreviewed; 463 AA.
AC A0A244E767;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
DE Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
GN Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
GN ORFNames=A8M77_22200 {ECO:0000313|EMBL:OUM00236.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM00236.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUM00236.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUM00236.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(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:0000256|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:0000256|HAMAP-Rule:MF_00834};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00834}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00834}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUM00236.1}.
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DR EMBL; LYMK01000029; OUM00236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244E767; -.
DR OrthoDB; 3398487at2; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000195166; Unassembled WGS sequence.
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; 3.90.1150.10; 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 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00834}; Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00834}; Reference proteome {ECO:0000313|Proteomes:UP000195166};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00834};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00834}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 128..129
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 267
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 331..332
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT SITE 31
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
SQ SEQUENCE 463 AA; 50416 MW; 0F78462DAF73BCF5 CRC64;
MPSLNPPSPP TAPSRNADWQ QRSRRHVWHP CTQSIRLEAV PPLPIARGEG VWLIDHDGRR
YLDATSSWWV NLFGHAHPAI NAALREQLDT LPHVMLAGCT HAPAVELAER LSALTGHALG
HCFYASDGAS AVEIALKMSF HAWRNAGRGG KRGFVALRGG YHGETLGALH VTDVAVFRDA
YAPLLRDVHL APSPDARGGR PGEDAPAVAR RAADALDALL AERHDSIAAV IVEPLVQCAA
GMAMHDPEYL RRVRAACDRH GVHLIADEIA VGCGRSGSFF ACEQAGIWPD FLCLSKGISG
GYLPLALVMT REAIYQGFVD EDVARSFLHS HSYTGNALAC RAALATLDLF EREDVLSRNR
GRAARILQRL REGLDPSRAE HLRQRGMITA FDVRQSGPRF AERFHLAARR QGLLMRPIGS
TVYLMPPYVI GDAEIDRLVE GTLATLDAVA ASRTAEDRDV ALA
//
