ID A0A1F8G2R2_9BACT Unreviewed; 377 AA.
AC A0A1F8G2R2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Polysaccharide biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3F25_00465 {ECO:0000313|EMBL:OGN19561.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_12_FULL_45_19b.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802689 {ECO:0000313|EMBL:OGN19561.1, ECO:0000313|Proteomes:UP000177478};
RN [1] {ECO:0000313|EMBL:OGN19561.1, ECO:0000313|Proteomes:UP000177478}
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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {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:OGN19561.1}.
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DR EMBL; MGKD01000013; OGN19561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8G2R2; -.
DR STRING; 1802689.A3F25_00465; -.
DR Proteomes; UP000177478; Unassembled WGS sequence.
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: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 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 377 AA; 42029 MW; 88F01832611EA575 CRC64;
MKYPIAKPYI GKEEKAVVAK VLRSGVLSIG PEVVAFEKAF ALKLGTKFAC AVSSGTAGLH
LTMLAAGLKK GDEVLTSPFS FIASANAILY VGATPVFVDI NPVSFNIDPD KIEEKITTKT
KAILVVHIFG QSADMKPILK LANKYKLKVI EDACESLNAS YHGKKVGTFG ESAVFAFYPN
KQMTTGEGGM IVTNDRSVDA LCRSLRNQGR SGNMQWLDHE RLGYNYRLDE MSAALGRVQL
QKLDWLIAEK RRIAALYKKH LAPYQKFLLL PRIISGNIHS WFVYVINIKN PLIKRDAVIE
DLEKLGISTK AYLPSIHLFS FYKKLFKYKR GDFPVSEAVS DCSLALPFYI GLKEKDIKII
SNIVVATLEK HEKYLQK
//
