ID C6WBT7_ACTMD Unreviewed; 426 AA.
AC C6WBT7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACU37504.1};
GN OrderedLocusNames=Amir_3615 {ECO:0000313|EMBL:ACU37504.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU37504.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU37504.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU37504.1; -; Genomic_DNA.
DR RefSeq; WP_015802392.1; NC_013093.1.
DR AlphaFoldDB; C6WBT7; -.
DR STRING; 446462.Amir_3615; -.
DR KEGG; ami:Amir_3615; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000002213; 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; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; 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:ACU37504.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Transferase {ECO:0000313|EMBL:ACU37504.1}.
SQ SEQUENCE 426 AA; 44294 MW; 578E1B0CD21F6454 CRC64;
MDTTTQGTTH HQDTTGGDLL AAYRAHLSAG RASLGEMFGG FWETASSGAT VRTSDGESFV
NCAGYGVFIL GGTHPHVTEA VVAQVRANPL ATRLLLEPVS AAAAKALVDV CPPGLSKVHF
VGSGTEATET AIKMARANGK RRLITTANGY HGKTLGSLSV TARSVYQEKF QPLLPDVTVV
PYGDVDAMEA ALRDGPPACV IVEPVQGEGG VVFPPDGYLA ALGRLRTEHD AFLVIDEILT
GLGRLGRWWG HDPEAVTPDV MLVGKGLSGG VVPVAAAVAT PAAYAPFDKD PFLHTSTFSA
APVAAAAAKA AIEAIVMEDA VAKAAKLGAE LKHRIAESAA RTCPHLVAEV RGEGLLIGVE
MRDPGLAGEL VLELIDGRVL VNHSMNNSHV LRLTPPATIT ADELDHVATT FDRALSTLAG
RFPASS
//
