GenomeNet

Database: UniProt/TrEMBL
Entry: Q5QZ15_IDILO
LinkDB: Q5QZ15_IDILO
Original site: Q5QZ15_IDILO 
ID   Q5QZ15_IDILO            Unreviewed;       431 AA.
AC   Q5QZ15;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   26-NOV-2014, entry version 67.
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   AltName: Full=7,8-diaminononanoate synthase {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   ECO:0000313|EMBL:AAV82165.1};
GN   OrderedLocusNames=IL1325 {ECO:0000313|EMBL:AAV82165.1};
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82165.1, ECO:0000313|Proteomes:UP000001171};
RN   [1] {ECO:0000313|EMBL:AAV82165.1, ECO:0000313|Proteomes:UP000001171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC   {ECO:0000313|Proteomes:UP000001171};
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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: S-adenosyl-L-methionine + 8-amino-7-
CC       oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
CC       diaminononanoate. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- COFACTOR:
CC       Note=Pyridoxal phosphate. {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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE017340; AAV82165.1; -; Genomic_DNA.
DR   RefSeq; YP_155714.1; NC_006512.1.
DR   ProteinModelPortal; Q5QZ15; -.
DR   SMR; Q5QZ15; 1-427.
DR   STRING; 283942.IL1325; -.
DR   EnsemblBacteria; AAV82165; AAV82165; IL1325.
DR   GeneID; 3173790; -.
DR   KEGG; ilo:IL1325; -.
DR   PATRIC; 22140725; VBIIdiLoi21852_1326.
DR   HOGENOM; HOG000020209; -.
DR   KO; K00833; -.
DR   OMA; PWQERRG; -.
DR   OrthoDB; EOG6QVRHN; -.
DR   BioCyc; ILOI283942:GI0U-1334-MONOMER; -.
DR   UniPathway; UPA00078; UER00160.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   PANTHER; PTHR11986; PTHR11986; 1.
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 {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:AAV82165.1};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001171};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:AAV82165.1}.
FT   REGION      112    113       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   REGION      310    311       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING      52     52       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     145    145       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     246    246       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     275    275       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     309    309       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     393    393       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE         17     17       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     275    275       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
SQ   SEQUENCE   431 AA;  47807 MW;  675C2506AB3093A4 CRC64;
     MSKSDIEFDR QHIWHPYTSM LNPLPAYKVE SAKGCRLTLD TGHEVVDGMS SWWAVIHGYR
     NPRLDAVAHR QIDKMSHVMF GGITHQPAID LARRLIELTP EPLQRVFIAD SGSVSVEVAI
     KMALQFWLAQ ERPEKHRLLT IKGGYHGDTF KAMSVCDPVN GMHHLFNRAI NSQLFAEAPR
     LTPDDDWAET AGDELRHWFE QHHHELAAVI LEPVVQGAGG MRFYHPEYLR LIRQLCDDFD
     VLLIADEIAT GFGRTGKLFA CEHAGITPDV LCVGKALTGG YMTLAATLTT KQVAETIGHG
     PGGGALMHGP TFMGNPLACA VAAESLAIIA EGKWQQQVAE IEAQLKQQLL PLAECDAVKD
     ARVFGAIGVL EMHHPIDVAI AQKRFVELGV WIRPFGRLLY IMPPYVISTN ELSRLTVAMK
     DYVETQSSIK A
//
DBGET integrated database retrieval system