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Database: UniProt
Entry: A0A0R2TMN3_9FLAO
LinkDB: A0A0R2TMN3_9FLAO
Original site: A0A0R2TMN3_9FLAO 
ID   A0A0R2TMN3_9FLAO        Unreviewed;       396 AA.
AC   A0A0R2TMN3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:KRO86427.1};
GN   ORFNames=ABR90_07655 {ECO:0000313|EMBL:KRO86427.1};
OS   Cryomorphaceae bacterium BACL29 MAG-121220-bin8.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX   NCBI_TaxID=1655598 {ECO:0000313|EMBL:KRO86427.1, ECO:0000313|Proteomes:UP000051665};
RN   [1] {ECO:0000313|EMBL:KRO86427.1, ECO:0000313|Proteomes:UP000051665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL7 MAG-121220-bin8 {ECO:0000313|EMBL:KRO86427.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-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 class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KRO86427.1}.
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DR   EMBL; LICI01000358; KRO86427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2TMN3; -.
DR   Proteomes; UP000051665; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KRO86427.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KRO86427.1}.
SQ   SEQUENCE   396 AA;  44287 MW;  8BBBDF60BE6A3E4D CRC64;
     MKKKFIKYQA QTTNHPIGLE VSYAKGSYIY DSENKKYLDF VAGISASNLG HRNKAISKAV
     IKQINKYWHV MVYGEFIQEP TVKLCEILSK NLPKSLSNTY LTNSGTEAIE AAMKLAKRVT
     GRAEIIAAKN GYHGSTQGSM SIMGFEERKR RYRPLLPGIK FIEFNNENDI DKISKNTAAV
     ILETIQGGAG FITPSEEYLK KIKNKCKELN TLLILDEIQP GIGRTGKLFA FEHYNVIPDI
     LVYGKGLGGG FPIGAISCSK KIMNSFKENP ILGHITTFGG HPVIAAAAYA NVKEIFETKI
     MSKVEEKEKL FKNYLKHPLI KEIRGKGLML ALILENKKIA NNLVIKCLEK GLILFYLLFE
     SKAVRITPPL TIKKSEIKKG CKIIIETLNQ INNSVH
//
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