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Database: UniProt/TrEMBL
Entry: A0A0M4DEL3_9ACTN
LinkDB: A0A0M4DEL3_9ACTN
Original site: A0A0M4DEL3_9ACTN 
ID   A0A0M4DEL3_9ACTN        Unreviewed;       427 AA.
AC   A0A0M4DEL3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=alanine--glyoxylate transaminase {ECO:0000256|ARBA:ARBA00013049};
DE            EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049};
GN   ORFNames=ABE83_05185 {ECO:0000313|EMBL:ALC26541.1};
OS   Streptomyces sp. CFMR 7.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1649184 {ECO:0000313|EMBL:ALC26541.1, ECO:0000313|Proteomes:UP000061366};
RN   [1] {ECO:0000313|EMBL:ALC26541.1, ECO:0000313|Proteomes:UP000061366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFMR-7 {ECO:0000313|EMBL:ALC26541.1,
RC   ECO:0000313|Proteomes:UP000061366};
RA   Sudesh K.;
RT   "Complete genome sequence of Streptomyces sp strain CFMR 7, a natural
RT   rubber degrading Actinomycetes isolated from Penang, Malaysia.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC         Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC         Evidence={ECO:0000256|ARBA:ARBA00001781};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP011522; ALC26541.1; -; Genomic_DNA.
DR   RefSeq; WP_019764650.1; NZ_VEHK01000014.1.
DR   AlphaFoldDB; A0A0M4DEL3; -.
DR   KEGG; scz:ABE83_05185; -.
DR   PATRIC; fig|1649184.3.peg.1118; -.
DR   Proteomes; UP000061366; Chromosome.
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:UniProt.
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; -; 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:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ALC26541.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALC26541.1}.
SQ   SEQUENCE   427 AA;  45621 MW;  940F2E56EE176022 CRC64;
     MSGLYERHLA VSPEWLALYY RHPIELTHGE GRYVWDADGN RYLDFFGGIL TTMTAHALPE
     VTKAVSEQAG RIIHSSTLYL NRPMVELAER IAHLSGIPDA RVFFTTSGTE ANDTALLLAT
     AYRRSNQILA MRNSYHGRSF SAVSITGNHA WSPTTLSPLQ TLYVHGGVRS RGPYAELSDD
     RFIRACVADL EDLLGHTREA AALIAEPIQG VGGFTSPPDG LFAAFREVLD RHGVLWISDE
     VQTGWGRTGE HFWGWQAHAE NGPPDMLTFA KGIGNGMSIG GVVARAEVMN CLDANSISTF
     GGSPVTMAAG LANLTYHLEH DLQGNARRVG GLLIERLRSV AAASDAVREV RGRGLMIGIE
     LVKPGTDEAD PEAAAAVLEA ARAGGLLIGK GGGHNTSVLR IAPPLTLTVA EAEEGASILA
     DALRAAG
//
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