ID A0A0C1UYC5_9ACTN Unreviewed; 430 AA.
AC A0A0C1UYC5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:KIE52495.1};
GN ORFNames=MB55_08265 {ECO:0000313|EMBL:KIE52495.1};
OS marine actinobacterium MedAcidi-G3.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE52495.1, ECO:0000313|Proteomes:UP000031370};
RN [1] {ECO:0000313|EMBL:KIE52495.1, ECO:0000313|Proteomes:UP000031370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE52495.1}.
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DR EMBL; JUEP01000016; KIE52495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1UYC5; -.
DR STRING; 1550402.MB55_08265; -.
DR Proteomes; UP000031370; Unassembled WGS sequence.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KIE52495.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KIE52495.1}.
SQ SEQUENCE 430 AA; 46321 MW; 9317DC0714B1F116 CRC64;
MSSTQELLQR YKAVMPSFVT PLYETPISIE RGEGGYVWDL EGNKYLDFFG GILTTMIGHS
APEVVKAIQE QASKVMHTST LYLNEQVVSF AEEVAAVSGI PDARVLFTTS GSEANDTAIL
LATNYRQSNQ ILAMRNSYHG RSLTTQAVTS HRSWLTSSYS GLDVHFVQGP YRLRSPFRDL
DDESFTQACV SDLAQLLDMT DAGGFAALIA EPIQGVGGFA TPPDGFFGAL HKVLEANNIL
FISDEVQTGW GRTGDHFWGY EAHGITPDIL TFAKGVGNGI TLAGCVARAE VMNVLDRTSF
TTFGGNPLSV AAGKATLKYV KDHNLQSNAA SRGLQMTNLL REPCNSTDWV AELRGKGLMQ
AIECVQPGSI EPNASAAARL IEECKNNGLL VGKGGLYGNV IRLTPMLNVS EAEMNEGCEI
ITSALNSTNG
//
