ID A0A3G3GPR8_9BACT Unreviewed; 375 AA.
AC A0A3G3GPR8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:AYQ33199.1};
GN ORFNames=DTQ70_13985 {ECO:0000313|EMBL:AYQ33199.1};
OS Runella sp. SP2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; Runella.
OX NCBI_TaxID=2268026 {ECO:0000313|EMBL:AYQ33199.1, ECO:0000313|Proteomes:UP000270973};
RN [1] {ECO:0000313|EMBL:AYQ33199.1, ECO:0000313|Proteomes:UP000270973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:AYQ33199.1,
RC ECO:0000313|Proteomes:UP000270973};
RA Jin H.M.;
RT "Genome sequence of Runella sp. SP1.";
RL Submitted (JUL-2018) 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 DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP031030; AYQ33199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3GPR8; -.
DR KEGG; rup:DTQ70_13985; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000270973; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:AYQ33199.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000270973};
KW Transferase {ECO:0000313|EMBL:AYQ33199.1}.
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 375 AA; 41209 MW; 6B6ED61F74A18022 CRC64;
MNKIWLSSPH MSGHEQKYVQ EAFETNWVAP LGPNVDGFEQ DLSRYVGVGH AAALSSGTAA
LHLALVMLGV GQGDVVICQS FTFAASANPI VYQGAMPVFV DSEWETWNIC PEALEEAIKG
ERAKGKKVKA VIAVHLYGMP AKIDEIVEVC ARYEVPLIED AAEGLGASWK GRKLGSFGKL
NILSFNGNKI ITTSGGGALL SDDEKLIQQS RFLATQARDN APHYQHSQIG YNYRMSNICA
GIGRGQMQVI DERVSQRRAS FAWYQQAFAG DERITFQPER EGSYANRWLS CIRVDATKTS
GVTREVLRIA LAAENIEARP LWKPMHLQPV FEGAPFYGGQ IAEILFDDGL CLPSGSNLTE
DDLQRVTKVL KRTLG
//
