ID I0HB92_ACTM4 Unreviewed; 374 AA.
AC I0HB92;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:BAL90279.1};
GN OrderedLocusNames=AMIS_50590 {ECO:0000313|EMBL:BAL90279.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL90279.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL90279.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; AP012319; BAL90279.1; -; Genomic_DNA.
DR RefSeq; WP_014445168.1; NC_017093.1.
DR AlphaFoldDB; I0HB92; -.
DR STRING; 512565.AMIS_50590; -.
DR KEGG; ams:AMIS_50590; -.
DR PATRIC; fig|512565.3.peg.5052; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_11; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000007882; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:BAL90279.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000007882};
KW Transferase {ECO:0000313|EMBL:BAL90279.1}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 40853 MW; E49F29AC5323782C CRC64;
MTTYVWNYLA EYESEREDIL EAVDQVFRSG RLVLGDSVQG FEREFAAYLG AGHCVGVDNG
TNAVKLALEA VGVTRGDEVI TVSNTAAPTV VAIDEIGAVP VFVDVRADDY LMDVGQVEAA
ITPRTRAIVP VHLYGQCVDM APLLRIAAKH DLRIVEDCAQ AHGARAGGRT AGTFGDAAAF
SFYPTKVLGA YGDGGAVVTA DAGVEAALRR LRYYGMEKTY YVVRTPGHNS RLDEVQAEIL
RRKLTRLDGY VKQRREVARR YAEGLAGLCG DGGLELPVVA PGNEHVYYVY VVRHSQRDRI
IEALAERHDI SLNISYPWPV HTMSGFAHLG VPRGALPVTE RLAGQIFSLP MYPSLEPALQ
DRVIDALHDV IRTL
//