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Database: UniProt
Entry: K2DH61_9BACT
LinkDB: K2DH61_9BACT
Original site: K2DH61_9BACT 
ID   K2DH61_9BACT            Unreviewed;       365 AA.
AC   K2DH61;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKD85844.1};
GN   ORFNames=ACD_37C00596G0009 {ECO:0000313|EMBL:EKD85844.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD85844.1};
RN   [1] {ECO:0000313|EMBL:EKD85844.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD85844.1}.
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DR   EMBL; AMFJ01014107; EKD85844.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2DH61; -.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2}.
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   365 AA;  40825 MW;  2D8D67DEDD842813 CRC64;
     MNVPVANPII DERELELVIK TVKSGWISSA GENISKFEDK FAEFCNTKYA ITTSNGTSAL
     HLCLVAYSIG PGDEVIVPSM TFVATANAVV YTGAKPVFVD SEFDTWNIDP ENIESKITPK
     TKAIIPVHLY GHPAKMDKII KIAQKYNLII IEDAAEAHGA RYNNKIVGSI GNAGCFSFYG
     NKIITTGEGG MITTSNKAIA DKIRTLRNHG SSPERKYYYP ELGFNYRMTN IQAAIGLAQL
     EKITDNIERK KEIHATYCEY LQPLHNKITM QPNAEWAESV FWMFSILLAS NGKISRDSLI
     DILHKKGIES RPFFFPLHKY IRFNNKDKLP VSEYLGNCGI SLPSGPKLSR KEIRYVCDEI
     ISILD
//
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