ID A0A1M6JTW2_9CLOT Unreviewed; 367 AA.
AC A0A1M6JTW2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Perosamine synthetase {ECO:0000313|EMBL:SHJ50099.1};
GN ORFNames=SAMN02745912_00150 {ECO:0000313|EMBL:SHJ50099.1};
OS Paramaledivibacter caminithermalis DSM 15212.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Paramaledivibacter.
OX NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHJ50099.1, ECO:0000313|Proteomes:UP000184465};
RN [1] {ECO:0000313|EMBL:SHJ50099.1, ECO:0000313|Proteomes:UP000184465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15212 {ECO:0000313|EMBL:SHJ50099.1,
RC ECO:0000313|Proteomes:UP000184465};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FRAG01000001; SHJ50099.1; -; Genomic_DNA.
DR RefSeq; WP_073146442.1; NZ_FRAG01000001.1.
DR AlphaFoldDB; A0A1M6JTW2; -.
DR STRING; 1121301.SAMN02745912_00150; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000184465; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000184465}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 367 AA; 41946 MW; BC0C09F4B5B39841 CRC64;
MKDIIHVASP ILNGNEKKYV NECLDTTWIS SKGKYVEKFE EEFKNFCNTK HAISCTNGTV
ALHLALLAFD IGPGDEVIVP TLTYIATANA VTYCGAKPVF VDSEPDTWNI DPNRIEEKIN
SNTKGIIVVH LYGHPVDMDL VIKIAKKYNL FVIEDVAEAH GAFYKGKATG SMGDISTFSF
FGNKIITTGE GGMVVTNDDK LNEKMRMLKS QGMDTVKRYW HPVVGYNYRM TNIQAAIGLG
QLENISWHLK KRREIVDLYY KYLENLSEYI KFQAEKNWAI HSYWMFSILL KDTVKVSRNK
FIELLKIDGI ETRPVFYPVH TMPPYKETEE KYPIAEKLSK RGINLPTHAL LKEEDIAYIS
IKIKKYC
//
