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Database: UniProt
Entry: B6ABQ4_CRYMR
LinkDB: B6ABQ4_CRYMR
Original site: B6ABQ4_CRYMR 
ID   B6ABQ4_CRYMR            Unreviewed;       669 AA.
AC   B6ABQ4;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase family protein {ECO:0000313|EMBL:EEA05806.1};
DE   SubName: Full=Bifunctional dethiobiotin synthetase/adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:DAA33947.1};
DE            EC=2.6.1.62 {ECO:0000313|EMBL:DAA33947.1, ECO:0000313|EMBL:EEA05806.1};
DE            EC=6.3.3.3 {ECO:0000313|EMBL:DAA33947.1, ECO:0000313|EMBL:EEA05806.1};
GN   Name=bioDA {ECO:0000313|EMBL:DAA33947.1};
GN   ORFNames=CMU_028160 {ECO:0000313|EMBL:EEA05806.1};
OS   Cryptosporidium muris (strain RN66).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN   [1] {ECO:0000313|EMBL:EEA05806.1, ECO:0000313|Proteomes:UP000001460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN66 {ECO:0000313|EMBL:EEA05806.1,
RC   ECO:0000313|Proteomes:UP000001460};
RA   Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA   da Silva J.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:DAA33947.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RN66 {ECO:0000313|EMBL:DAA33947.1};
RX   PubMed=20713166; DOI=10.1016/j.fgb.2010.08.004;
RA   Magliano P., Flipphi M., Sanglard D., Poirier Y.;
RT   "Characterization of the Aspergillus nidulans biotin biosynthetic gene
RT   cluster and use of the bioDA gene as a new transformation marker.";
RL   Fungal Genet. Biol. 48:208-215(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
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DR   EMBL; BK007853; DAA33947.1; -; Genomic_DNA.
DR   EMBL; DS989727; EEA05806.1; -; Genomic_DNA.
DR   RefSeq; XP_002140155.1; XM_002140119.1.
DR   AlphaFoldDB; B6ABQ4; -.
DR   STRING; 441375.B6ABQ4; -.
DR   EnsemblProtists; EEA05806; EEA05806; CMU_028160.
DR   GeneID; 6994734; -.
DR   VEuPathDB; CryptoDB:CMU_028160; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   OrthoDB; 884390at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001460; Unassembled WGS sequence.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03109; DTBS; 1.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00834; BioA; 1.
DR   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR005815; BioA.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00508; bioA; 1.
DR   NCBIfam; TIGR00347; bioD; 1.
DR   PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF3; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:EEA05806.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Ligase {ECO:0000313|EMBL:EEA05806.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001460};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEA05806.1}.
SQ   SEQUENCE   669 AA;  76159 MW;  19587D989693B05E CRC64;
     MTNIFITATD TDVGKTTISA LLCLHYGCSY HKVIQSGDLE NSDSMTISQL VPNVKIYPEQ
     IKLKKSLSPN LSAEFENKEI SLSDFNFDLL SQDNVIIEGV GGILVPLSDK LDIIDLIEYS
     GMVTLLVVPS RLGMINQARM ALNLLKNRNI NIIGFVTNGE YRPDDFNVIS RLTDTNHLFH
     IPTMKIINHE SLKSLKIPTD LFCSIEKNEH LGICKKISEY NTNNQLLCLN LCERDSKMIW
     HPYTQHGIES EFKCFISGSG SFLIDEEGNK WLDLISSWWV ITFGHCDKKL SEAITKQVKT
     LDHIVFAGYT HEPAIKLAEM LLDLNSQYFH KVFYSDNGST AIEVALKAVI HYYQNRGQRN
     RISWLALEGG YHGDTFGAMS VGYSSNYFKP YYEFLFQKIH FIPYPESYDD TTEEQWQIDC
     ELSLNKAKYI ISFIGKENIA GMIIEPLIQG ASGMRQTRPE FLNKLLSICK DNEIIVIFDE
     IFTGFGRTGT LFAYQQLKYI PDILCLSKGI TGGVLPLSVT LFPQYIYDAF VSDNISTAFI
     HGHSFTANPI SCSAAIANLS RINSENTFAL IQKINDANSA FILELKKKFE DRIYNYFTKG
     PLCVFSLKDK YENYGLNFNI IIKKCLERKY LIIRPLGNRI YLLPPYEIDI ETLQQAHKLI
     IEALFELNI
//
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