ID A0A0F2C8R2_9MICO Unreviewed; 376 AA.
AC A0A0F2C8R2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative pyridoxal phosphate-dependent aminotransferase EpsN {ECO:0000313|EMBL:KJQ55093.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:KJQ55093.1};
GN Name=epsN {ECO:0000313|EMBL:KJQ55093.1};
GN ORFNames=RS85_01152 {ECO:0000313|EMBL:KJQ55093.1};
OS Microbacterium sp. SA39.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ55093.1, ECO:0000313|Proteomes:UP000033425};
RN [1] {ECO:0000313|EMBL:KJQ55093.1, ECO:0000313|Proteomes:UP000033425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ55093.1,
RC ECO:0000313|Proteomes:UP000033425};
RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (JAN-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|ARBA:ARBA00037999, 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:KJQ55093.1}.
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DR EMBL; JXRU01000029; KJQ55093.1; -; Genomic_DNA.
DR RefSeq; WP_052703438.1; NZ_JXRU01000029.1.
DR AlphaFoldDB; A0A0F2C8R2; -.
DR STRING; 1263625.RS85_01152; -.
DR PATRIC; fig|1263625.4.peg.1168; -.
DR Proteomes; UP000033425; 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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:KJQ55093.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033425};
KW Transferase {ECO:0000313|EMBL:KJQ55093.1}.
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 376 AA; 39790 MW; C213D9F29A5FC53D CRC64;
MSERIYMSSP DVGEAEEQAV VAAMRSGWIA PLGPDVDAFE RELAERVGVA HAVALSSGTA
ALHLGLLTLG VKPGDVVLTS SMTFAATANA IVYTGAEPYF IDADPATGNM DPSLLREALV
ELRDAGETVS AIVPVDLLGK AVDYTAILAI ADEFGVPVLS DAAESLGATH RGRAAGSFGR
ASVVSFNGNK IMTTSGGGML LTDDADIAQH VRYLATQARQ PVVHYEHTDI GYNYRMSNLL
AALGRAQLTR LDAMIARRRE MRELYKQLFA DVDGVEVFGA EGDEADNVWL TSILVDAETT
GWEPSALAAA LAEDSIESRP LWKPMHAQPV FAGARSKVSG ASDTLFARGL TLPSGSALTP
EQRERVVAAI RGFLAS
//
