BIOA_CORGL
ID BIOA_CORGL Reviewed; 423 AA.
AC P46395;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=Cgl2604, cg2885;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=MJ233;
RX PubMed=8161820; DOI=10.3109/10425179309015630;
RA Hatakeyama K., Hohama K., Vertes A.A., Kobayashi M., Kurusu Y., Yukawa H.;
RT "Genomic organization of the biotin biosynthetic genes of coryneform
RT bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium
RT flavum.";
RL DNA Seq. 4:177-184(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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:8161820}.
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; D14083; BAA03167.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99997.1; -; Genomic_DNA.
DR EMBL; BX927155; CAF21266.1; -; Genomic_DNA.
DR PIR; I40336; I40336.
DR RefSeq; NP_601805.1; NC_003450.3.
DR RefSeq; WP_011015243.1; NC_006958.1.
DR AlphaFoldDB; P46395; -.
DR SMR; P46395; -.
DR STRING; 196627.cg2885; -.
DR KEGG; cgb:cg2885; -.
DR KEGG; cgl:Cgl2604; -.
DR PATRIC; fig|196627.13.peg.2540; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_11; -.
DR OMA; VAVKMCL; -.
DR BRENDA; 2.6.1.19; 960.
DR BRENDA; 2.6.1.62; 960.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000000582; 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 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..423
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120365"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 111..112
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 307..308
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT SITE 18
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 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT CONFLICT 30
FT /note="K -> N (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> R (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> A (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="R -> H (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="T -> A (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="L -> V (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="L -> V (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..298
FT /note="STPN -> RSPE (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> V (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="A -> E (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="R -> K (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="E -> K (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..352
FT /note="QHL -> RCI (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="T -> R (in Ref. 1; BAA03167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 45741 MW; 88773BED8418632D CRC64;
MENPSLRELD HRNIWHPYAA PGVRNRLVTK TDGVFLTLED GSTVIDAMSS WWSAIHGHGH
PRLKAAAQKQ IDTMSHVMFG GLTHEPAIKL THKLLNLTGN SFDHVFYSDS GSVSVEVAIK
MALQASKGQG HPERTKLLTW RSGYHGDTFT AMSVCDPENG MHSLWKGTLP EQIFAPAPPV
RGSSPQAISE YLRSMELLID ETVSAIIIEP IVQGAGGMRF HDVALIEGVA TLCKKHDRFL
IVDEIATGFG RTGELFATLS NGLQPDIMCV GKALTGGFMS FAATLCTDKV AQLISTPNGG
GALMHGPTFM ANPLACAVSH ASLEIIETGM WQKQVKRIEA ELIAGLSPLQ HLPGVADVRV
LGAIGVIEME QNVNVEEATQ AALDHGVWIR PFGRLLYVMP PYITTSEQCA QICTALHAAV
KGK
