ID A0A0S8A788_9BACT Unreviewed; 336 AA.
AC A0A0S8A788;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:KPJ94538.1};
DE Flags: Fragment;
GN ORFNames=AMS18_03485 {ECO:0000313|EMBL:KPJ94538.1};
OS Gemmatimonas sp. SG8_17.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703355 {ECO:0000313|EMBL:KPJ94538.1, ECO:0000313|Proteomes:UP000051607};
RN [1] {ECO:0000313|EMBL:KPJ94538.1, ECO:0000313|Proteomes:UP000051607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_17 {ECO:0000313|EMBL:KPJ94538.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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:KPJ94538.1}.
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DR EMBL; LJNM01000045; KPJ94538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8A788; -.
DR PATRIC; fig|1703355.3.peg.3432; -.
DR Proteomes; UP000051607; 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; 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; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 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:KPJ94538.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KPJ94538.1}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPJ94538.1"
SQ SEQUENCE 336 AA; 36607 MW; 7A6B52C38C8C5823 CRC64;
LCKIFFGAPT GSDAVEAAVK LAKYNSGRYP MIAFEGAYHG MTAGALSLCS GAPFKGDFLP
LLPEVHFVPY SYCYRCPFNR EPTSCDLECG KFLEHVVEDS HSGVGKPAAI LVEAIQGEGG
SIVPDDRFIP KVREICTKYG ILMIVDEIQA GFCRTGKMFS FEHTGTVPDI VTMSKALGGV
GFPISAVAYR EELDTWPPGK HIGTFRGNMI AYAGGAAAIQ FMQQHGLADH AMRLGNLVLD
WLKQLEGDSE IIGETRGKGL MLGVEFVKDK VSKEPAPELA AQVRTLCHKR GVLIEIGGHY
FNVARFLPPL VLTEELARKG FDIFAESVRE LEKTGR
//
