ID K0K7T1_SACES Unreviewed; 433 AA.
AC K0K7T1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:CCH32934.1};
GN OrderedLocusNames=BN6_56750 {ECO:0000313|EMBL:CCH32934.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH32934.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH32934.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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; HE804045; CCH32934.1; -; Genomic_DNA.
DR RefSeq; WP_015103046.1; NC_019673.1.
DR AlphaFoldDB; K0K7T1; -.
DR STRING; 1179773.BN6_56750; -.
DR KEGG; sesp:BN6_56750; -.
DR PATRIC; fig|1179773.3.peg.5715; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_1_11; -.
DR OrthoDB; 5342089at2; -.
DR BioCyc; SESP1179773:BN6_RS27350-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
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: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 Aminotransferase {ECO:0000313|EMBL:CCH32934.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW Transferase {ECO:0000313|EMBL:CCH32934.1}.
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 433 AA; 46009 MW; 54E64C0625F3EFD2 CRC64;
MRVDEGETRL AAFGGSAAVP RELRSLPWPV VTEADRAAVL AVLGGDAMVS NVDGETAVSA
LEQRWAALCG AEHCVATSNG TTALALAFAA LGIGPGDEVV VPALSFIASG LAPLHQMAVP
VFADIDPVDF TLDAESAAAL ITPRTAAIMP VHLHGAPADM DAIGALARRH GLAVVEDAAQ
AHGARWRGRP VGSLGDAAAF SLQVTKNLPT CGEGGLLTLA DADAAGRARM ARQFGEVIEP
GRDRDYVAHL LGWNHKMNAV QAAFALSQLD RFAEYERARQ RNVTAFLARL AELPGLLVPT
IAPDSKHAWH ILRFRFDAEA MGVDGVTPES LRRALHRLLR AEGVPVSRYQ VLTLPRQRVF
TDRVGFGRGR PWSGAAPEPS APVPVAESVV AGTLTLQKRH LHPEAGPALA RYADGFEKVW
RRLDLVARMA KVA
//
