ID A0A126T6Q4_9GAMM Unreviewed; 402 AA.
AC A0A126T6Q4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:AMK77762.1};
GN ORFNames=JT25_014975 {ECO:0000313|EMBL:AMK77762.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK77762.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK77762.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK77762.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP014476; AMK77762.1; -; Genomic_DNA.
DR RefSeq; WP_036276969.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A126T6Q4; -.
DR STRING; 1538553.JT25_014975; -.
DR KEGG; mdn:JT25_014975; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000030512; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AMK77762.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030512};
KW Transferase {ECO:0000313|EMBL:AMK77762.1}.
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 237
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 402 AA; 43777 MW; DEA6033325738F95 CRC64;
MFDGFIRLVR EIYQTEQFIP LHEPRFAGNE KQYLLDVIDS TFVSSVGPYV GEFETKIAEY
TGAKHAIATV NGTAALHVAL LLAGVEPGEE VITQAVTFVA TCNAIHYCGA EPVFVDVDAA
TLGLSPAALT NFLDCHGERR DGGIYNKTSG KRIAACLPMH SFGHPCDMLG LLQVCEGYGI
PVVEDAAEAL GSRIVGSNSF APSAVSANEL ASTPATKYAK HCGALGKLGV LSFNGNKIIT
TGGGGMILTD DDELARHAKH LTTTAKLPHA WRFAHDQIGY NYRMPNLNAA LGLAQLEQLP
AFVERKRALA QRYLDWAQTN GAQIVVEPTG ARSNYWLNAL LLDDVRQRNA FLEYSNAQGV
MTRPLWELMA DLPMYKHCQR DSLTQSRRLA ERLVNVPSSV VL
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