ID D1ABB8_THECD Unreviewed; 458 AA.
AC D1ABB8;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACY97154.1};
GN OrderedLocusNames=Tcur_1578 {ECO:0000313|EMBL:ACY97154.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY97154.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY97154.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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; CP001738; ACY97154.1; -; Genomic_DNA.
DR RefSeq; WP_012851938.1; NC_013510.1.
DR AlphaFoldDB; D1ABB8; -.
DR STRING; 471852.Tcur_1578; -.
DR KEGG; tcu:Tcur_1578; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_0_11; -.
DR OrthoDB; 3204291at2; -.
DR Proteomes; UP000001918; 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:ACY97154.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW Transferase {ECO:0000313|EMBL:ACY97154.1}.
SQ SEQUENCE 458 AA; 50457 MW; A9093B6EEAF55B51 CRC64;
MTDPTQDPLQ SAARDHLWMH FTRHSSLIDG GEVPVIVRGD GPYVYDDKGK RYLDGLAGLF
TTQVGHGRQE LAQAAAKQAA ELAFFPLWSY AHPKAIELAE RLAALAPGEL NRVFFTTGGG
EAVESAWKLA KQYFKLTGKP TKHKVISRAI AYHGTTQGAL SLTGLPAIKA PFEPLVPSAF
RVPNTNIYRA PVHGDDPEAF GRWAADRIEE AILFEGPDTV AAVFLEPVQN AGGCFPPPPG
YFQRVREICD RYDVLLVSDE VICAYGRLGT MFGAQRYDYQ PDIITFAKGI TSGYAPLGGM
LVTDRLFEPF RKGTTTFAHG YTFGGHPVSA AVALANLDLF EREDLLGHVQ RNEALFRSTL
EKLLDLPIVG DVRGAGYFYG IELVKDKATK ESFTDEESER LLRGFVDKAL FEAGLYCRAD
DRGDPVVQLA PPLICDRSHF EEMEQILRAV LSEASNRL
//
