ID Q5QZ15_IDILO Unreviewed; 431 AA.
AC Q5QZ15;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
DE EC=2.6.1.62;
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase;
DE AltName: Full=7,8-diaminononanoate synthase;
DE AltName: Full=Diaminopelargonic acid synthase;
GN Name=bioA; OrderedLocusNames=IL1325;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
CC oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
CC diaminononanoate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily.
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; DRVFYAD; -.
DR BioCyc; ILOI283942:GI0U-1357-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:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA: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 PANTHER; PTHR11986:SF8; PTHR11986:SF8; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Biotin biosynthesis; Complete proteome; Cytoplasm;
KW Pyridoxal phosphate; S-adenosyl-L-methionine; Transferase.
FT REGION 112 113 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 310 311 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 52 52 Substrate (By similarity).
FT BINDING 145 145 Substrate (By similarity).
FT BINDING 246 246 Pyridoxal phosphate (By similarity).
FT BINDING 275 275 Substrate (By similarity).
FT BINDING 309 309 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 393 393 Substrate (By similarity).
FT SITE 17 17 Participates in the substrate recognition
FT with KAPA and in a stacking interaction
FT with the adenine ring of SAM (By
FT similarity).
FT MOD_RES 275 275 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
