ID C4RFU1_MICS3 Unreviewed; 412 AA.
AC C4RFU1;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:EEP70203.1};
GN ORFNames=MCAG_00530 {ECO:0000313|EMBL:EEP70203.1};
OS Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP70203.1, ECO:0000313|Proteomes:UP000010307};
RN [1] {ECO:0000313|Proteomes:UP000010307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413
RC {ECO:0000313|Proteomes:UP000010307};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT 39149.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG657738; EEP70203.1; -; Genomic_DNA.
DR RefSeq; WP_007071483.1; NZ_GG657738.1.
DR AlphaFoldDB; C4RFU1; -.
DR STRING; 219305.MCAG_00530; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_4_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000010307; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EEP70203.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000010307};
KW Transferase {ECO:0000313|EMBL:EEP70203.1}.
SQ SEQUENCE 412 AA; 44628 MW; AFA00FE58958E5A8 CRC64;
MTGPAPLDLS QSQALLRRAV AVDATLAYEG YVLARDRLVD GAYPLYGERA SGAHIWDVDG
NRYLDLILAY GTIILGHADP VVSEAVMREI RDGFAITLRK RVQVELAELL TAVIPHAEKV
FLLKTGSDAT SAAVRLSRVH TGRNRVIRWG YNGWHDWCAT RPGGVPTEAQ AVVDTFDYND
LDSLRTVFER HPGEVACLLM MPFEVDPPAP GFLAGAAELA HEHGALFVLD EMRSGFRMAP
GGAQERYGVR ADLVTFSKAM ANGYPISALV GREEVMRAVG EVHISSTFHV NGAEMAAAVA
TISQLRDGTI LKHVEHLGER LQAGLAAQLA EHGLPGRVLG VPQMPFLRFT DPDDAARGRA
HDAFYTETTR RGLLLHPNHH WYVSGAMTDE DVDAALEATA SGFRAAAVAA HG
//