ID   A0A258WU99_9SPHI        Unreviewed;       434 AA.
AC   A0A258WU99;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OYZ31770.1};
GN   ORFNames=B7Y24_08000 {ECO:0000313|EMBL:OYZ31770.1};
OS   Sphingobacteriales bacterium 16-39-50.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1970581 {ECO:0000313|EMBL:OYZ31770.1, ECO:0000313|Proteomes:UP000216983};
RN   [1] {ECO:0000313|EMBL:OYZ31770.1, ECO:0000313|Proteomes:UP000216983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16-39-50 {ECO:0000313|EMBL:OYZ31770.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {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:OYZ31770.1}.
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DR   EMBL; NCHA01000005; OYZ31770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258WU99; -.
DR   Proteomes; UP000216983; Unassembled WGS sequence.
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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:OYZ31770.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:OYZ31770.1}.
SQ   SEQUENCE   434 AA;  48323 MW;  62C187618748ADA7 CRC64;
     MEIRSYNKSA KLLERAKRVL AGGVSSEFRK YNHPHALFYT HGKGSRIYDA DGNEYLDFTL
     SQGPLILGHS HPHVLKSINE YSAGGQLFAG QHIREIELAE KINQLIPTAE LMRFCLDGSE
     AIHTAFRLAR AKTGKKKFLR FEGHYHGWLD NVCWGISAPS EEALGSRESP EVFPWSDGLA
     ISTRDECIVI PWNDAELLKA TVEKHYKELA AIITEPVMCN NGCIMPNPGF LQMIRELCSE
     YNITFILDEV ITGFRLSLGG AQQFFNIQPD LSIFAKALAS GYPISVIAGK KEWMRLIEEA
     KVIHAGTMNS GNATIAAALA TIEVLEKEHP YGRMFSLGKE LMQGIRDAAK QTGHNLLVQG
     PGPMFNLSFT EAKEINEFRA TLSCNKAKLG SFIAGMHNEG VRIIGRGLWY ISAVHTQDDI
     NFAIEKVRKV LKNI
//