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Database: UniProt
Entry: A0A0G3V4L4_9ACTN
LinkDB: A0A0G3V4L4_9ACTN
Original site: A0A0G3V4L4_9ACTN 
ID   A0A0G3V4L4_9ACTN        Unreviewed;       388 AA.
AC   A0A0G3V4L4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Putative PLP-dependent enzyme {ECO:0000313|EMBL:AKL74395.1};
GN   ORFNames=IMCC26256_112127 {ECO:0000313|EMBL:AKL74395.1};
OS   Actinobacteria bacterium IMCC26256.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1650658 {ECO:0000313|EMBL:AKL74395.1, ECO:0000313|Proteomes:UP000035517};
RN   [1] {ECO:0000313|EMBL:AKL74395.1, ECO:0000313|Proteomes:UP000035517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC26256 {ECO:0000313|EMBL:AKL74395.1,
RC   ECO:0000313|Proteomes:UP000035517};
RA   Kim S.;
RT   "Genome sequencing of freshwater Actinobacteria.";
RL   Submitted (MAY-2015) 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; CP011489; AKL74395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3V4L4; -.
DR   STRING; 1650658.IMCC26256_112127; -.
DR   KEGG; abai:IMCC26256_112127; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000035517; Chromosome.
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: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:UP000035517}.
FT   REGION          327..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   388 AA;  41034 MW;  9A47BFD1EFD21555 CRC64;
     MKKLAVLGGE KSFPDGVAFV RPPAPPLEEV VARLAPSYSQ GSLTNGPLVR ELEDSVAERL
     GVRNVVAVSS CTTGLMLSVA GLAEFGEISG PVIMPSFTFS AGPHAVAWSN LGVRFVECDP
     LSFQIDLAHT SMHLEGAGAI MATHVFGAPC RPEQVEAMGK SAGIPVLFDA AHGFGALRHG
     RPLGGFGEVE VFSMTPTKPL VAGEGGLVCT DRDDLAEYLR LAREYGNPGD YNTRFIGLNG
     RLSEMHAAIA LASISHIDEH LETRRRLAGR YSDGILAIPG VRTQAVDSED LSTYKDFTIA
     IDAGDFGVSR DQLVTALSAE GIDTRNYFDP PVHRQDSHAS RSPSDLPVTD AVSKTVVSLP
     LYPALTDAVV DQIVEIIAGV GESAASLN
//
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