ID A0A1F8KNK8_9CHLR Unreviewed; 452 AA.
AC A0A1F8KNK8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:OGN75883.1};
GN ORFNames=A2X25_01700 {ECO:0000313|EMBL:OGN75883.1};
OS Chloroflexi bacterium GWB2_49_20.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN75883.1, ECO:0000313|Proteomes:UP000178842};
RN [1] {ECO:0000313|EMBL:OGN75883.1, ECO:0000313|Proteomes:UP000178842}
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 -!- 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:OGN75883.1}.
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DR EMBL; MGMF01000002; OGN75883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8KNK8; -.
DR STRING; 1797612.A2X25_01700; -.
DR Proteomes; UP000178842; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OGN75883.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:OGN75883.1}.
SQ SEQUENCE 452 AA; 50445 MW; 50DAB5F2016E2935 CRC64;
MPILNRARLK RLIQEEIQRF QQEHPKSNEL YLRARQSMQG GVPMLWMIRW PGSFPIFVKN
ARGAHFEDVD GHSYIDFCLG DTGAMTGHSP VESVEAIRNQ VGNGITLMLP MEDAIWVGEE
LQRRFGLKFW QFTLTATDAN RFAIRMARHI TGRPKILVFN YCYHGSVDET FITLDEKGLP
GPRSGNLGPP INPIETSRVV EFNDIPALEE ALIHGDVAAV LAEPVMTNIG IIHPQPGYHD
ALRKLTRKYG SCLIIDETHT ICTSPGGYTG KFGLDPDFLT CGKPLASGIP AGVYGFTQQV
ADAFWARIQH DESDVGGVGG TLAGNALSIA AIRATLEHVL TQAMYDRCEA LADHYEQGIL
DCISDYELPW IVKRLGFRVE YWFCETAPIN GGEANAAVDS DLDRFMHLWA LNRGILMTPF
HNMALIAADT TEEDIEYHTR IFREAVQTLI AE
//
