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Database: UniProt
Entry: A0A1C6R7U2_9ACTN
LinkDB: A0A1C6R7U2_9ACTN
Original site: A0A1C6R7U2_9ACTN 
ID   A0A1C6R7U2_9ACTN        Unreviewed;       378 AA.
AC   A0A1C6R7U2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Perosamine synthetase {ECO:0000313|EMBL:SCL13114.1};
GN   ORFNames=GA0070616_0132 {ECO:0000313|EMBL:SCL13114.1};
OS   Micromonospora nigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL13114.1, ECO:0000313|Proteomes:UP000199699};
RN   [1] {ECO:0000313|EMBL:SCL13114.1, ECO:0000313|Proteomes:UP000199699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL13114.1,
RC   ECO:0000313|Proteomes:UP000199699};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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|RuleBase:RU004508}.
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DR   EMBL; FMHT01000002; SCL13114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6R7U2; -.
DR   STRING; 145857.GA0070616_0132; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000199699; Unassembled WGS sequence.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199699}.
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   378 AA;  39972 MW;  1506E4E2475FBCDF CRC64;
     MTPEYPRTAA PPDLAGLDEA VVADLARLLT RMPDPAGSAH GAALERELAA TTGVRHAVAV
     SSGTAALHTA LRALHIGPGD DVLVPALSVI MSVAPVVHAG ARPIFVDCDP TGTDLDYDDL
     SRKVTPAAKA VLPVHLWGRP GDPARLARAA AEHGLAVVED ACQAQGSRAG GRLAGTTGDV
     GCFSLKDGKV LWSGEGGYLL TDRDDIAQRA RSFRSHQQPP PPEDGHPAEV GYNYRLAEPL
     ALLARANLAR FDTLAARRRH QACLLADLLT GAPGIDVTDV PARRGWNGYS FLATVTLDEP
     RAFCQHLARC GVPNSVGTFG LIPADRRPAL APFTTAPCPH AAAVVDRTLA VILTDHDDEQ
     RITGYAQTIM KEARRWTP
//
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