ID A0A1Q4GVD0_9PROT Unreviewed; 373 AA.
AC A0A1Q4GVD0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:OJZ20328.1};
GN ORFNames=BGP21_07740 {ECO:0000313|EMBL:OJZ20328.1};
OS Thiobacillus sp. 65-29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1895862 {ECO:0000313|EMBL:OJZ20328.1, ECO:0000313|Proteomes:UP000186483};
RN [1] {ECO:0000313|EMBL:OJZ20328.1, ECO:0000313|Proteomes:UP000186483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65-29 {ECO:0000313|EMBL:OJZ20328.1};
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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:OJZ20328.1}.
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DR EMBL; MKWN01000010; OJZ20328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4GVD0; -.
DR STRING; 1895862.BGP21_07740; -.
DR Proteomes; UP000186483; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR30244:SF9; PROTEIN RV3402C; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OJZ20328.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:OJZ20328.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 373 AA; 41360 MW; 8041B5B4BB85453C CRC64;
MMPPTESRKI LVTQPVLPPL DAFIPYLEQI WESRQLTNSG PFHQQLEQAL RDYLGVSQIA
LFTNGTLALV TALQALRITG EVITTPYSFV ATAHSLLWNG IRPVFVDIDP VTLNLDPDRI
EAAITPHTTA IMPVHCYGHP CEVERIQKIA DNYGLKVIYD AAHAFGVHGQ DGNILNHGDL
SVLSFHATKV FNTFEGGAIV CHDAKTKQRI DHLKNFGFVD EVTVVAPGIN GKMSEIMAAF
GLLQLQGIDA ALHKRQTIDA RYRAALADVK GITCLPVREG RANYAYFPIL VGPEYPLSRD
TLYERLREHG IYARRYFYPL ISDFPMYRGM PSAAPENLPV AKAAAERVIC LPIHPGLSED
QVDLVLRVVV EAD
//
