ID A0A368JNY5_9BACT Unreviewed; 385 AA.
AC A0A368JNY5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RCR68364.1};
GN ORFNames=DUE52_16535 {ECO:0000313|EMBL:RCR68364.1};
OS Larkinella punicea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Larkinella.
OX NCBI_TaxID=2315727 {ECO:0000313|EMBL:RCR68364.1, ECO:0000313|Proteomes:UP000253383};
RN [1] {ECO:0000313|EMBL:RCR68364.1, ECO:0000313|Proteomes:UP000253383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zzj9 {ECO:0000313|Proteomes:UP000253383};
RA Zhou Z., Wang G.;
RT "Genome analysis of Larkinella rosea.";
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}.
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:RCR68364.1}.
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DR EMBL; QOWE01000013; RCR68364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368JNY5; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000253383; Unassembled WGS sequence.
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:RCR68364.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:RCR68364.1}.
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 385 AA; 41938 MW; 84C4FD2E16905C51 CRC64;
MIPEIYLSSP HLGDLELQYV QEAFAANWVA PVGPHIDAFE RELCIETGAA HAAALSSGTS
ALHLSLVLLG VSPGDEVICQ SFTFAASANP IVYQGATPVF IDSEADTWNM CPDALEMALK
DRLARGKRPK AVIVVNLYGM PAKLDALLKI CHQYEVPLVE DAAESFGSTY NDKPCGSFGK
LAVLSFNGNK IITTSGGGAL LSEDEALIKR ARFLATQARD PAPYYQHSSI GYNYRISNVC
AGIGRGQLRI LADRVAQRRA NYAYYFEHLI KLPGFAFQPE PDPCFSNRWL TCITVDPDLS
GGITCEAIRL ALAEKRIEAR PLWKPMHQQP VFAGLPYYGS GVSNRLFKTG LCLPSGSNLT
REQITKVVSC VEETVEVAYL ADGKN
//