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Database: UniProt
Entry: D8GN07_CLOLD
LinkDB: D8GN07_CLOLD
Original site: D8GN07_CLOLD 
ID   D8GN07_CLOLD            Unreviewed;       396 AA.
AC   D8GN07;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative LPS biosynthesis-related protein {ECO:0000313|EMBL:ADK13631.1};
GN   OrderedLocusNames=CLJU_c05490 {ECO:0000313|EMBL:ADK13631.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK13631.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK13631.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP001666; ADK13631.1; -; Genomic_DNA.
DR   RefSeq; WP_013237231.1; NZ_LITS01000023.1.
DR   AlphaFoldDB; D8GN07; -.
DR   STRING; 748727.CLJU_c05490; -.
DR   KEGG; clj:CLJU_c05490; -.
DR   PATRIC; fig|748727.19.peg.1626; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_0_3_9; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000001656; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR020026; PseC.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03588; PseC; 1.
DR   PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}.
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   396 AA;  44477 MW;  2153B04049A39F79 CRC64;
     MNELAINGGR PIRKTYLSYG RQDIDEEDIE SVVKVLKGDF LTTGPSVREF EKKVSDYVGA
     KHAVAVASGT AALHMACFAA GIKEGDEVIV SPITFAASAN CVLYCGGTPV FADIDPKTYN
     IDPKEIEKKV TSKTKAIIPV DFTGQSVDID EIRRIAGKNN LIIIEDSAHA LGSEYKGKKV
     GTKAQMTEFS FHPVKPVTSG EGGMVVTDDD ELYKKMILFR SHGITRDKDL ITHNEGPWYY
     EQIDLGYNYR ITDIQCALGA SQMNKIDKFI SRRRDIAKTY NEAFKDVAEI TTPCEAEFSN
     SGWHLYVIKL NLEKLTCTRK EIFEALQAEN IGVNVHYLPV YLHPYYQKLG YQKGLCKNAE
     ELYERMITIP LFPKMTDEDV SDVIDGVKKV INYYKR
//
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