ID Q0RQU2_FRAAA Unreviewed; 464 AA.
AC Q0RQU2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:CAJ60081.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CAJ60081.1};
GN OrderedLocusNames=FRAAL1423 {ECO:0000313|EMBL:CAJ60081.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ60081.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ60081.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CT573213; CAJ60081.1; -; Genomic_DNA.
DR RefSeq; WP_011602618.1; NC_008278.1.
DR AlphaFoldDB; Q0RQU2; -.
DR STRING; 326424.FRAAL1423; -.
DR KEGG; fal:FRAAL1423; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_4_0_11; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR049704; Aminotrans_3_PPA_site.
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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAJ60081.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Transferase {ECO:0000313|EMBL:CAJ60081.1}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 48815 MW; 41A0D3E34C342574 CRC64;
MTTTPATPAT PATPASPDVA GRSEAYADDR RHVFHSWSAQ ASLDPVVVAG AEGSWFWDES
GRRYLDFSSQ LVNANIGHQH PAVVEAIAAQ ARSLTTVAPF HAHEVRSRAA RLIAERAPGD
LDRVFFTNGG AEATENAVRI ARLATGRHKI LAAYRSYHGA TGGSITLTGE PRRWPSEPGI
PGVVHFFGPY PYRSPFHAVD AAEESDRALA HLAEVIALEG PATIAAIIVE PVVGTNGILV
PPPGYLAGVR ELCDTHGIVF IADEVMSGFG RCGEWFAVDH WGVVPDLICF AKGVNSGYVP
LGGVILAPHL ADAFAERPYP GGLTYSGHLL GCAAAVASIE AFEAEGILDH VRMLGTEVIG
PGLAKLAANH PSVGEVRGLG VFWALELVRD GATREPLVPF NAAGPAAAPM GAVAAACRER
GLWPFTHFNR VHVVPPCTIS VADARTGLAI LDEALTIADG FTTA
//
