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Database: UniProt
Entry: N0E4H6_9MICO
LinkDB: N0E4H6_9MICO
Original site: N0E4H6_9MICO 
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
//
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