ID A0A1F9ZWP3_9BACT Unreviewed; 436 AA.
AC A0A1F9ZWP3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Alanine--glyoxylate aminotransferase {ECO:0000313|EMBL:OGS56282.1};
GN ORFNames=A3J79_10510 {ECO:0000313|EMBL:OGS56282.1};
OS Elusimicrobia bacterium RIFOXYB2_FULL_62_6.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797970 {ECO:0000313|EMBL:OGS56282.1, ECO:0000313|Proteomes:UP000177734};
RN [1] {ECO:0000313|EMBL:OGS56282.1, ECO:0000313|Proteomes:UP000177734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGS56282.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGVP01000205; OGS56282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9ZWP3; -.
DR Proteomes; UP000177734; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OGS56282.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:OGS56282.1}.
SQ SEQUENCE 436 AA; 47320 MW; E295B8F687934B34 CRC64;
MTNAEATKKY TNAELTKKYK EFLYPSVITY YAEPLPLVSG KGCRVYDAEG NEYLDFFGGI
LTVSVGHSNP AVIDRTAAQL KKLQHVSTLY PTAPAAELAE RLAGITPGDI KKSFFTNSGS
EADEMAVLTA QHYTGAQEII ALRHSYSGRS LLTMNMTAHS NWRVSRTLVA GIKHAHAAYC
YRCPFKLNYP ACDMACAHDL EELIQTETCG KIAALLAEPI LGVGGFVVPP KEYFKVVVDI
VHKYGGLFIA DEVQTGWGRT GGKWFGIEHF GVVPDIMTSA KGMANGIPIG WTATTAKIAE
SLKGLTISTF GGNPVSCAAA HATIDYINEA KIMDNVTKMG DYLRGEMLAM QKEFKCIGDV
RGMGLMIGVE LVSDRKTKAP DAKAVVKIFE ETKKDGLLIG KGGLYGNVLR ISPPMNVTKA
EIDEALKTLH KAFKTI
//