ID   C9ZGG2_STRSW            Unreviewed;       428 AA.
AC   C9ZGG2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Aminotransferase class III {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=SCAB_18021 {ECO:0000313|EMBL:CBG68932.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68932.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG68932.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG68932.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN554889; CBG68932.1; -; Genomic_DNA.
DR   RefSeq; WP_012999656.1; NC_013929.1.
DR   AlphaFoldDB; C9ZGG2; -.
DR   STRING; 680198.SCAB_18021; -.
DR   GeneID; 24307882; -.
DR   KEGG; scb:SCAB_18021; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
SQ   SEQUENCE   428 AA;  45829 MW;  1AAB0A0F9FDDD07D CRC64;
     MTDELLGRHK AVLPDWLALY YADPLEITHG EGRHVWDAAG TRYLDFFGGI LTTMTAHALP
     EVTKAVSEQA GRIIHSSTLY LNRPMVELAE RIAQMSGIPD ARVFFTTSGT EANDTALMLA
     TTHRRSNQIL AMRNSYHGRS FSAVGITGNK GWSPTSLSPL QTLYVHGGVR TRGPYADLSD
     ADFITACVAD LEDLLGHGRP PAALIAEPVQ GVGGFTSPPD GLYAAFREVL QRHGVLWIAD
     EVQTGWGRTG DNFWGWQAHG QNGPPDILTF AKGIGNGMSI GGVVARSEVM NCLDSNSIST
     FGGTQITMAA GLANLNYLIE HDLQGNARRV GGLLIERLRA ITAQIPEVKE VRGRGLMIGI
     ELVKPGTDEA NPEAASAVLE AARREGLLIG KGGGHNTSAL RIAPPLSLTV AEAEEGAEAL
     ERALRSIR
//