ID A0A0M9CBZ0_9ACTN Unreviewed; 434 AA.
AC A0A0M9CBZ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=2,2-dialkylglycine decarboxylase {ECO:0000313|EMBL:KOY49119.1};
GN ORFNames=ISGA_12285 {ECO:0000313|EMBL:KOY49119.1};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:KOY49119.1, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:KOY49119.1, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY49119.1,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:KOY49119.1}.
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DR EMBL; APHK02000096; KOY49119.1; -; Genomic_DNA.
DR RefSeq; WP_053778395.1; NZ_CP132196.1.
DR AlphaFoldDB; A0A0M9CBZ0; -.
DR STRING; 1241906.ISGA_12285; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000011989; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989}.
SQ SEQUENCE 434 AA; 46026 MW; 71CCC8F44D784BFE CRC64;
MAPTDPQPVT APDLTRHLIR YGGTISPELI GRAEGSFVHT AGGRRILDFT SGQMSAILGH
SHPEIVATVS HQIATLDHLF SGMLSAPVLD LAERLTDTLP DPLDKVILLT TGAESNEAAI
RMAKLVTGRH EIVSFARSWH GMTAAAAAAT YSAGRGGYGP VGPGNFALPT PDAFRPDFTH
PDGTLDWQRQ LDFGFSLIDA QSTGSLAACI VEPILSSGGV IDLPPGYLAA LADKCRQRGM
LLILDEAQTG LCRTGSWYAF ERDGVVPDIL TLSKTLGAGL PLAATVTSSE IERIAHDRGF
LFFTTHVSDP LPAAVGNTVL DVLQRDRLDV RAAEAGDLLR GGLADIARRH RVVGDIRGRG
LLQGLELTDT DAATSDELGA AITRRCYELG LHMNVVQLPG LGGTFRIAPP LTASDDELRL
GLEILEQAIA ETTA
//
