ID A0A066ZT16_HYDMR Unreviewed; 416 AA.
AC A0A066ZT16;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KDN95429.1};
GN ORFNames=EI16_03775 {ECO:0000313|EMBL:KDN95429.1};
OS Hydrogenovibrio marinus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=28885 {ECO:0000313|EMBL:KDN95429.1, ECO:0000313|Proteomes:UP000027341};
RN [1] {ECO:0000313|EMBL:KDN95429.1, ECO:0000313|Proteomes:UP000027341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-110 {ECO:0000313|EMBL:KDN95429.1,
RC ECO:0000313|Proteomes:UP000027341};
RA Cha H.J., Jo B.H., Hwang B.H.;
RT "Draft genome sequence of Hydrogenovibrio marinus MH-110, a model organism
RT for aerobic H2 metabolism.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KDN95429.1}.
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DR EMBL; JMIU01000001; KDN95429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066ZT16; -.
DR STRING; 28885.EI16_03775; -.
DR Proteomes; UP000027341; Unassembled WGS sequence.
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:KDN95429.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000027341};
KW Transferase {ECO:0000313|EMBL:KDN95429.1}.
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 232
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 416 AA; 45407 MW; 46E6031B641AA485 CRC64;
MTADNLKNVT SEAQSDRWQS LANAIRNHYQ VAESDFVPLH APCFDETEKE LLNACIDSTF
VSSVGEFVGA FEEQIADFTG AKHAVAVVNG TMGLFLGLKV VGVKAGDLVL TQSLTFVATP
NAIKMLGADP VFVDVAPKTM GLSAEALAEF LSTQTYQQNG KCFHKASHRL ISACAPMHTL
GFPMEIEQVV SLCHEYGIKV VEDAAESLGS FVNGVHTGTF GDVGVFSFNG NKVITTGGGG
MLVTNNPDIA AHAKHLSTTA KIPHQWLFEH DEIGYNLRMP NLNAALGVAQ MKKLPSFLAE
KHQLALQYQD WVSSTQTSGS PNLVDFGADY RQNFPDNLPN YWLNACVLNS NEDRDAFLSE
FNGANLQTRP LWTPMHRLEI YQNELRGDMT HTEFFAERVV NVPSGVICPP PVELAL
//
