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Database: UniProt
Entry: I0R2V9_9MICO
LinkDB: I0R2V9_9MICO
Original site: I0R2V9_9MICO 
ID   I0R2V9_9MICO            Unreviewed;       497 AA.
AC   I0R2V9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Aspartate aminotransferase family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IMCC13023_06740 {ECO:0000313|EMBL:EIC92195.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC92195.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT   member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIC92195.1}.
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DR   EMBL; AJKR01000002; EIC92195.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0R2V9; -.
DR   STRING; 1081644.IMCC13023_06740; -.
DR   PATRIC; fig|1081644.3.peg.681; -.
DR   eggNOG; COG0161; Bacteria.
DR   Proteomes; UP000054510; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054510}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  55727 MW;  598A6351F4EEC6DD CRC64;
     MAIQENNKTK SLRDLFSSKK KSHVSNASKS DFPIVHAMAA GQEVGDKALQ KSAKKHLWMH
     FTRHSPYNKI DMTIIQKADG HYLTDSKGRR VIDGLSGLFT VNAGHGRQEL ADAAAKQTME
     LDFMPLWSYA HPRAVELAER LISYAPKDLT RIFFTTGGGE AVESAWKIAK QYFKMTGKPL
     KHKVISRQTA YHGTSHGALS ITGIAAFKQM FEPLVPSTFR IPNTNWYRAD SRFKTEDEFA
     LWAANRLEEV ILFEGPDTVA AFFVEPIQNA GGCFTAPNSY FKRIREICDK YDVILVADET
     ITGFGRTGEM FGSQRYDINP DMMITAKAIT SGVAPLGALF IKEKYFTPFN EGTVTLAHGY
     TFAAHPVACA VALANLDIYD KERLVDNVRI NSPIFRKTLE KLKDLPIVGD VRGDGYFFAI
     ELVRNQETKE SLTREESEKI LRGFLNNALY EQGLYCRADD RGDPVIQLAP PLTCGPKEFE
     EIEQILRSVL IEAGKRL
//
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