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
//