ID N0E4H6_9MICO Unreviewed; 385 AA.
AC N0E4H6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:CCH70771.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CCH70771.1};
GN Name=epsN {ECO:0000313|EMBL:CCH70771.1};
GN ORFNames=BN10_670016 {ECO:0000313|EMBL:CCH70771.1};
OS Phycicoccus elongatus Lp2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH70771.1, ECO:0000313|Proteomes:UP000013167};
RN [1] {ECO:0000313|EMBL:CCH70771.1, ECO:0000313|Proteomes:UP000013167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lp2 {ECO:0000313|EMBL:CCH70771.1,
RC ECO:0000313|Proteomes:UP000013167};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH70771.1}.
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DR EMBL; CAIZ01000138; CCH70771.1; -; Genomic_DNA.
DR RefSeq; WP_010850614.1; NZ_HF570956.1.
DR AlphaFoldDB; N0E4H6; -.
DR STRING; 1193181.BN10_670016; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_11; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000013167; 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:CCH70771.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000013167};
KW Transferase {ECO:0000313|EMBL:CCH70771.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 385 AA; 40603 MW; F6985310D1B2F0EB CRC64;
MRERIYLSSP DVTEAEEQAL ARAISSGWVA PLGPEVDAFE AELADYCGRR HAVALSSGTA
ALHLGLITLG VGPGDLVLTS TMTFAATANA ITYVGAEPVF VDCDATGNMD AGLLEEAFER
CAGGGQRVAA VLPVDLLGKV VDHARVDDIA SAHGVPVLAD AAESLGATRD GRPAASFGNV
AAVSFNGNKV MTTSGGGALL TDDAHLAQRV RYLATQARQP VVHYEHTEIG YNYRLSNLLA
ALGRAQLARL DGMVQRRRQH RLGYLELFDG VAGVSAFGEP SGLAGGPTHD NWWLTSVIID
PSVAGFAPED LRLALSDADI EARPLWKPMH LQPVFAGARA VLDGTSERLF STGLSLPGGS
VLDDGQMQRI HAVITSFLEG RRATR
//