ID A0A087BMM5_9BIFI Unreviewed; 462 AA.
AC A0A087BMM5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KFI72275.1};
DE EC=4.2.3.2 {ECO:0000313|EMBL:KFI72275.1};
GN ORFNames=BMIN_0167 {ECO:0000313|EMBL:KFI72275.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI72275.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI72275.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI72275.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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:KFI72275.1}.
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DR EMBL; JGZD01000009; KFI72275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BMM5; -.
DR STRING; 1693.BMIN_0167; -.
DR eggNOG; COG0160; Bacteria.
DR Proteomes; UP000029014; Unassembled WGS sequence.
DR GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; IEA:UniProtKB-EC.
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; 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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KFI72275.1};
KW Lyase {ECO:0000313|EMBL:KFI72275.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029014};
KW Transferase {ECO:0000313|EMBL:KFI72275.1}.
SQ SEQUENCE 462 AA; 50598 MW; 3B22E5BD4FA8EF4B CRC64;
MTQERRHNDG NSIDHYGYEQ FQARDGGRLD PRTRELTRER SVLGDAYRLF YRTPVHLVKG
RGSHLWDADG VEYLDVYNNV ASVGHCHPRV VEAMTRQASE LNTHTRYLHE NILHYAEDIL
STMPDPLDRV MFQCTGSEAN DLAVRVAQAY TGGEGVIVTH EAYHGNSALT SKLSPALGTA
QDLGLTMRMI PTPDTYRVSV DGIRGSQCDA ATFGAWMADR VRDAVADMNR HGIKFAALLA
DSIFSSDGVY PDPVGYLQPV IDVVHELGGV WIADEVQPGF TRTGDAFWGF ERQGIVPDLV
TSGKPMANGL PTSLMAARHE ILEPFAGSIP YFNTFGGNPV CMAAAQAVLD VMRDEDTMGN
SKKVGAVFKA AVEGLKDSHP CIGDVRGAGL YIGCEIVKPG TTDPDQASAL DILETLRQNH
VLTSVCGRYG NILKLRPPLV FSEDDVDWFM SAFSTTLDSL DK
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