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Database: UniProt
Entry: A0A1F9ZWP3_9BACT
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Original site: A0A1F9ZWP3_9BACT 
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}.
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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
//
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