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Database: UniProt
Entry: R1HQI0_9PSEU
LinkDB: R1HQI0_9PSEU
Original site: R1HQI0_9PSEU 
ID   R1HQI0_9PSEU            Unreviewed;       368 AA.
AC   R1HQI0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:EOD65825.1};
GN   ORFNames=H480_24727 {ECO:0000313|EMBL:EOD65825.1};
OS   Amycolatopsis vancoresmycina DSM 44592.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD65825.1, ECO:0000313|Proteomes:UP000014139};
RN   [1] {ECO:0000313|EMBL:EOD65825.1, ECO:0000313|Proteomes:UP000014139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD65825.1,
RC   ECO:0000313|Proteomes:UP000014139};
RA   Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT   "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOD65825.1}.
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DR   EMBL; AOUO01000367; EOD65825.1; -; Genomic_DNA.
DR   RefSeq; WP_003096470.1; NZ_AOUO01000367.1.
DR   AlphaFoldDB; R1HQI0; -.
DR   PATRIC; fig|1292037.4.peg.4676; -.
DR   eggNOG; COG0399; Bacteria.
DR   OrthoDB; 5342089at2; -.
DR   Proteomes; UP000014139; Unassembled WGS sequence.
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:EOD65825.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:EOD65825.1}.
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         178
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   368 AA;  39386 MW;  5267D4B42511EE5B CRC64;
     MIPITVVDVR DAEDLVVEVL RSGAIAQGPM VKRFEDAFAA VSGTKHAIAV NNGTTALVAA
     LQVLDLKPGD EVVTSPFTFV ATLNAILEAG ATVRFADIRR DDFAIDPDAV ARAVTDRTKV
     LMPVHLYGQT ADMGKLAPLA AEHGLQVIED SAQAVGASFE GKQAGSFGIG CFSLYATKNI
     TTAEGGVITT DDDALADKLR VLRNQGMRAR YQYEVAGHNY RMTDLHAAVG IPQLAKLDQL
     TAARQANAKR LSEGLAGTPG LDVPQVLPGR EHVWHQYTVL VGPHAFLSRD ELAAALTERG
     IGNGIYYPKI VFDYECYAGH DLIPGARVED FPVARAVSEQ ALSLPVHPHL TESDLDTIIE
     TVREVLGA
//
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