ID A0A1S1Y6I8_9GAMM Unreviewed; 394 AA.
AC A0A1S1Y6I8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=BJL95_20965 {ECO:0000313|EMBL:OHX37146.1};
OS Methylomonas sp. LWB.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1905845 {ECO:0000313|EMBL:OHX37146.1, ECO:0000313|Proteomes:UP000180009};
RN [1] {ECO:0000313|EMBL:OHX37146.1, ECO:0000313|Proteomes:UP000180009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LWB {ECO:0000313|EMBL:OHX37146.1,
RC ECO:0000313|Proteomes:UP000180009};
RA Stephenson J., Kumaresan D., Hillebrand-Voiculescu A.M., Murrell J.C.;
RT "Draft genome sequence of the methane oxidising bacterium Candidatus
RT Methylomonas sp. LWB isolated from Movile Cave.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:OHX37146.1}.
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DR EMBL; MKMC01000012; OHX37146.1; -; Genomic_DNA.
DR RefSeq; WP_064029686.1; NZ_MKMC01000012.1.
DR AlphaFoldDB; A0A1S1Y6I8; -.
DR Proteomes; UP000180009; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF1; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAC; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481};
KW Reference proteome {ECO:0000313|Proteomes:UP000180009};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 31..378
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 44079 MW; 1064805E6A7FBB08 CRC64;
MEEFHRISRL PPYVFNIVNE LKAKARADGE DIIDFGMGNP DQPTPPHILN KMLEVAQRDD
THRYSVSKGI PRLRKAICGW YKRRFDVDLD FNTEAIVTIG SKEGLSHLAL ATLGPGDVVL
VPNPAYPIHP YGVVIAGADI RHVPLTPGTD FFEELHKGIA ECWPKPKMLI LNFPGNPTCQ
CVELDFFEKV VAICKEHNIW IVHDIAYADI VFDGYVAPSI LQVEGAKDIA VEFFSLSKSY
NMPGWRVGFM CGNPTLVAAL TRIKSYMDYG TFTPIQVAAI TALEGPQDCV AEIRDMYKAR
RDVLCDGLNA MGWHVEKPKA TMFVWAKIPD AYQGMGSIEF AKKLIIDAKV AVSPGIGFGQ
HGDDHIRFSL IENEHRTRQA LRSIRNMLKK DNVV
//
