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Database: UniProt
Entry: J3CN80_9FLAO
LinkDB: J3CN80_9FLAO
Original site: J3CN80_9FLAO 
ID   J3CN80_9FLAO            Unreviewed;       380 AA.
AC   J3CN80;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Aminotransferase, LLPSF_NHT_00031 family {ECO:0000313|EMBL:EJL74896.1};
GN   ORFNames=PMI13_00776 {ECO:0000313|EMBL:EJL74896.1};
OS   Chryseobacterium populi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1144316 {ECO:0000313|EMBL:EJL74896.1, ECO:0000313|Proteomes:UP000007509};
RN   [1] {ECO:0000313|EMBL:EJL74896.1, ECO:0000313|Proteomes:UP000007509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF314 {ECO:0000313|EMBL:EJL74896.1,
RC   ECO:0000313|Proteomes:UP000007509};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(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|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:EJL74896.1}.
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DR   EMBL; AKJY01000012; EJL74896.1; -; Genomic_DNA.
DR   RefSeq; WP_007840859.1; NZ_AKJY01000012.1.
DR   AlphaFoldDB; J3CN80; -.
DR   PATRIC; fig|1144316.3.peg.787; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000007509; 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; IPR026385; LegC-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR04181; NHT_00031; 1.
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:EJL74896.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Transferase {ECO:0000313|EMBL:EJL74896.1}.
FT   ACT_SITE        216
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   380 AA;  42698 MW;  64801174A777BB36 CRC64;
     MEHIQQMVSF IRDQYKTDQF IPLHEPRFRG NEKKYLNDTI DSTFVSSVGS YVNQFENMME
     DITGAAKAVA VVNGTSSLQV ALRLAGVQPG DEVITQALSF IATANAIAYN NASPIFLDVD
     LDTMGLSPKA VEAFLEEFGE IRDNGCFNKS TGKKIAACMP MHTFGFPVHM DELLEICSKW
     NIPVVEDSAE SLGSYYKGKH TGTLGLLGGF SFNGNKTVTC GGGGSIVTND VELARHAKYL
     TTTAKKPHPY EFFHDELGYN FRMPNLNAAL ACAQLEQLNT FIEDKRSLAL AYSELFKSLG
     IRFRQEIPDT KANYWLMCVE LENKIERENF LKLTNEQGIM TRPIWTLTYR LPMYEHCQRD
     AQTNAEFLEE RIVNIPSSVR
//
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