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Database: UniProt
Entry: C4RFU1_MICS3
LinkDB: C4RFU1_MICS3
Original site: C4RFU1_MICS3 
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
//
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