ID A0A1Q3QVL3_9BACT Unreviewed; 460 AA.
AC A0A1Q3QVL3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OJV43854.1};
GN ORFNames=BGO25_11930 {ECO:0000313|EMBL:OJV43854.1};
OS Acidobacteriales bacterium 59-55.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales.
OX NCBI_TaxID=1895690 {ECO:0000313|EMBL:OJV43854.1, ECO:0000313|Proteomes:UP000186822};
RN [1] {ECO:0000313|EMBL:OJV43854.1, ECO:0000313|Proteomes:UP000186822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=59-55 {ECO:0000313|EMBL:OJV43854.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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:OJV43854.1}.
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DR EMBL; MKSV01000003; OJV43854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3QVL3; -.
DR STRING; 1895690.BGO25_11930; -.
DR Proteomes; UP000186822; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OJV43854.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}; Transferase {ECO:0000313|EMBL:OJV43854.1}.
FT MOD_RES 261
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 460 AA; 50072 MW; 178EB584A058083B CRC64;
MSAELLDGFF RLLAEAQRRL DDGFTGLPAN PTPAMGEAVS AILSDVAVKL RDNYPYAHPL
YAGQMLKPPH PIARAAYALA MSVNPNNHAL DGGRASSAME IEAVAALAKM FHWPQHLGHL
TSGGTFANLE ALWIAGQLAP GKAIAASDQA HYTHSRISGV LGLPFIAIPS DETGRIDLQA
LEDILQTEEI GTVVVTLGTT ATGTVDPLDE ILKLRQRHRF RIHVDAAYGG YFTLAGNLSP
EARAAFDAVQ QVDSIVIDPH KHGLQPYGCG SVLFRDPSVG RFYKHDSPYT YFSSKDLHLG
EISLECSRAG ASAVALWATQ QLLPYTEGGI FARNLESSLT AALELHRRIV ANPGFAAPIF
PPELDIVFWT VRASTPALSS VFAQRVFEEA ARRDLHLALA QLPVRFFSPA CWRQAPQTET
VTCLRSVLMK PEHLKWIDQI WERLTAASMS VAVNTALEPN
//
