ID A0A127VJG2_9SPHI Unreviewed; 389 AA.
AC A0A127VJG2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AY601_4565 {ECO:0000313|EMBL:AMQ01402.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMQ01402.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMQ01402.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMQ01402.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP014504; AMQ01402.1; -; Genomic_DNA.
DR RefSeq; WP_068405486.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127VJG2; -.
DR KEGG; pcm:AY601_4565; -.
DR PATRIC; fig|188932.3.peg.4732; -.
DR OrthoDB; 9802872at2; -.
DR Proteomes; UP000071561; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481};
KW Reference proteome {ECO:0000313|Proteomes:UP000071561};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 27..379
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 389 AA; 42815 MW; D02D12C58C629849 CRC64;
MFQSQSVNLD ILKKRAFNLR WATVPEGVIP LTAADPDFPS APEIAESIIR FTQDRYLSYG
PAAGLPEFKE SLANYYTVKR NIPAVPGFIF PVDSAAFGIY LTCKAFLSPG DEAIIFDPVD
FLFRYSTEAV GGVAVPFAIP PGIDTVDFDN LERLITPKTR MICLCNPLNP TGKVFKKEEL
LQLGEIACKH GLIILSDEIW SDIVYTPNLY TSIASINEEI RNQTITVTGF SKSYGLAGLR
IGAVMASNQV HYDRLFEVSL HGSTIHGANI LSQVAATTAL NDCGYWLDEF LVHLQKMRDL
TVRELNATQG FKCISPEGCY VAFTNITGTG KSSKEIHQLL LDKAKVAVVP GAKEWFGEGA
EGFIRMSFAT SEDILNEALY NIKTTVNTL
//
