(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIR6_GEOS0

ID   A0A0F6BIR6_GEOS0        Unreviewed;       455 AA.
AC   A0A0F6BIR6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 27.
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   OrderedLocusNames=GY4MC1_0484 {ECO:0000313|EMBL:ADP73317.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73317.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73317.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73317.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC       adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
CC       (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
CC       animotransferase known to utilize SAM as an amino donor.
CC       {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-amino-7-oxononanoate + S-adenosyl-L-methionine = 7,8-
CC         diaminononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate;
CC         Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:57532,
CC         ChEBI:CHEBI:58500, ChEBI:CHEBI:59789; EC=2.6.1.62;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC       1/1. {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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002293; ADP73317.1; -; Genomic_DNA.
DR   RefSeq; WP_013400057.1; NC_014650.1.
DR   EnsemblBacteria; ADP73317; ADP73317; GY4MC1_0484.
DR   KEGG; gmc:GY4MC1_0484; -.
DR   KO; K00833; -.
DR   OMA; NGSSCIE; -.
DR   OrthoDB; 478143at2; -.
DR   BioCyc; GSP581103:G1GOQ-535-MONOMER; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000002034; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; A0A0F6BIR6.
DR   SWISS-2DPAGE; A0A0F6BIR6.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ADP73317.1};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000256|RuleBase:RU003560};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ADP73317.1}.
FT   REGION      116    117       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   COILED      204    224       {ECO:0000256|SAM:Coils}.
FT   COILED      341    368       {ECO:0000256|SAM:Coils}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     258    258       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     287    287       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     322    322       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     417    417       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE         20     20       Participates in the substrate recognition
FT                                with KAPA and in a stacking interaction
FT                                with the adenine ring of SAM.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   MOD_RES     287    287       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
SQ   SEQUENCE   455 AA;  51424 MW;  176C9630317B61DD CRC64;
     MRYSYEQLEQ WDKEYVWHPF TQMKTYVQEH PLIIERGSGS YLFDVNGNKY LDGYASLWVN
     VHGHNDPELN EALHMQIETI AHSTLLGSAN VPSILLAKKL VELWPGLSKV FYSDTGAAAV
     EIALKIAYQY WQNIDPVRYA KKTAFVSLRE AYHGDTIGAV SVGGMELYHR IFQPLLFERI
     EVPSPYVYRM SEYGNEQEIV QYCLQQLEHV LASEQERVAA VIVEPLVQGA AGIITHPRGF
     LKGVEALCRR YGVLLICDEV AVGFGRTGTM FACEQEQVTP DIVCLGKGIT GGYLPLAATL
     TTNQVYEAFL GEADENKTFY HGHTYTGNQL SCSVALKNIE LMEKRQLVEN VRKKAEFLAK
     KLEMLYELPI VGDIRQKGLM TGIEIVQDRN TKEIFPHSEM IEHRIILEAR KRGLIIRPLG
     PVLTFIPVLA MTEEQMETAV SILFDSIAEM AKAVR
//

If you have problems or comments...

PBIL Back to PBIL home page