ID A0A1G1Q0N5_9BACT Unreviewed; 379 AA.
AC A0A1G1Q0N5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Class V aminotransferase {ECO:0000313|EMBL:OGX47769.1};
GN ORFNames=A2243_00500 {ECO:0000313|EMBL:OGX47769.1};
OS Omnitrophica WOR_2 bacterium RIFOXYA2_FULL_38_17.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801873 {ECO:0000313|EMBL:OGX47769.1, ECO:0000313|Proteomes:UP000179162};
RN [1] {ECO:0000313|EMBL:OGX47769.1, ECO:0000313|Proteomes:UP000179162}
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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:OGX47769.1}.
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DR EMBL; MHHG01000057; OGX47769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1Q0N5; -.
DR Proteomes; UP000179162; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OGX47769.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:OGX47769.1}.
FT DOMAIN 27..325
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 379 AA; 40697 MW; F0F1F049A5047EAD CRC64;
MKRNLILAPG PTQIPPDLCA ALGKPIIHHR TPQFAQNLKD VIDGLQYVMQ TKNDVYILTS
SGTGAMEAAV CNLVGKGDKA ITVEGGKFGE RWTELCKVYG AEPQVIEVKW GTAVKPADIK
ALLDKDKSIK AVFVTLNETS TGVVSDIKSI AAVVKETNAV LVVDAISGLG VIDIKMDDWA
VDVIVSASHK GFMLPPGISF VAMNEKAYKL VEKCETPRYY FDLRKSKKVY NDPDTPFTPA
ISIVVALVDS LRKFKEEGLD KLFARYAKLA EATRAAAKAL GMTILAGDDC VSNAVTPIVL
PEGVAGGKVV KIMRDTYGVT VAGGQGYLKG KIVRIAHMGC VDEYDILTGI ACFEKALKDV
GYSFEMGAGV KAAQEVFNS
//
