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Database: UniProt
Entry: A0A0R0CBR8_9GAMM
LinkDB: A0A0R0CBR8_9GAMM
Original site: A0A0R0CBR8_9GAMM 
ID   A0A0R0CBR8_9GAMM        Unreviewed;       430 AA.
AC   A0A0R0CBR8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   31-JUL-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   ORFNames=ABB26_12695 {ECO:0000313|EMBL:KRG63345.1};
OS   Stenotrophomonas humi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG63345.1, ECO:0000313|Proteomes:UP000050864};
RN   [1] {ECO:0000313|EMBL:KRG63345.1, ECO:0000313|Proteomes:UP000050864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG63345.1,
RC   ECO:0000313|Proteomes:UP000050864};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus
RT   Stenotrophomonas.";
RL   Submitted (MAY-2015) 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: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRG63345.1}.
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DR   EMBL; LDJI01000024; KRG63345.1; -; Genomic_DNA.
DR   RefSeq; WP_057634692.1; NZ_LDJI01000024.1.
DR   EnsemblBacteria; KRG63345; KRG63345; ABB26_12695.
DR   PATRIC; fig|405444.3.peg.1636; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000050864; 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; 3.40.640.10; -; 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   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00508; bioA; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:KRG63345.1};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050864};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050864};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:KRG63345.1}.
FT   REGION      110    111       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   REGION      307    308       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING      50     50       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     143    143       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     244    244       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     273    273       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     306    306       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     390    390       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE         15     15       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     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
SQ   SEQUENCE   430 AA;  46792 MW;  6DB0C48BD51CACC5 CRC64;
     MLIDSFDREH LWHPYSALGS PVPVLKVARA DGVLLQLEDG PQLIDGMASW WCAIHGYNHP
     QLNQAAIEQL GRMSHVMFGG LTHEPAIALG KLLLEIVPKP LDAIFYADSG SVSVEVALKM
     AIQYQAARGV PRKNNIATTR SGYHGDTWNA MSVCDPVNGM HGLFGTSLPS RCFVPAPQTP
     FDGEWDAADI APVEQLFAER GGELAAFIIE PIVQGAGGMR FYHPQYLREL ARLCREHDVL
     LICDEIATGF GRSGRLFGCE HAGVTPDIMC IGKALTGGYM TLAATITRRE IADVIAAGEP
     GVFMHGPTFM ANPLACAVAL ASTQLLLSQD WQGRIASIEK TLHARLAPAR GLPQVADVRV
     LGAIGVIELK ASLRLDRIQQ RMLEQGIWIR PFGRLVYVMP PYVINDAQLQ QLCDGMVALV
     AGLEEEDMRA
//
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