ID A0A0G3H6S7_9CORY Unreviewed; 450 AA.
AC A0A0G3H6S7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:AKK07543.1};
DE EC=2.6.1.55 {ECO:0000313|EMBL:AKK07543.1};
GN ORFNames=CTEST_00365 {ECO:0000313|EMBL:AKK07543.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK07543.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK07543.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK07543.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP011545; AKK07543.1; -; Genomic_DNA.
DR RefSeq; WP_047252046.1; NZ_JAASJB010000003.1.
DR AlphaFoldDB; A0A0G3H6S7; -.
DR STRING; 136857.CTEST_00365; -.
DR KEGG; cted:CTEST_00365; -.
DR PATRIC; fig|136857.5.peg.72; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000035540; Chromosome.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
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:AKK07543.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000035540};
KW Transferase {ECO:0000313|EMBL:AKK07543.1}.
SQ SEQUENCE 450 AA; 49123 MW; 4855ACBB1F025331 CRC64;
MAQLTPEQGQ RAFDLDRAHV FHSWSAQGAL NPVPVAGGKN ATFWDFDGNE YLDFNSQMVN
VNLGHQHPTL IKAIQDQAAT LCTIGPAFAN DTRSEAARLI ASVAPEGLNH VFFTNGGAEA
VENAVKMARI HTGRDKIMAA YRSYHGATAT AITLTGEPRR FNNRHTDSGV VHFMGPYTYQ
SPFWSTSEEE ECERALAHLE QQIVLEGSHT IAAIIMEPVV GGMGVIVPPA GYLKGLKALC
EKYGILFIAD EVMVGFGRCG TWFTVDNFDV TPDLITFAKG SNSGYVPLGG VIMSDAIYET
FVDRVFPGGL TYSGHPLACA PVVATFQVFE EEQLLDHVND LAERVIRPRL EAMRDKHAIV
GDVRGLGMFW AIELVKNKDT REPLVPYNAQ GADLQPMNEF AAACKKAGLW PFIGMNRTHV
APPLTITEED LVRGLDIIDE ALGGLAQYAD
//
