ID A0A1F8F8Z7_9BACT Unreviewed; 374 AA.
AC A0A1F8F8Z7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:OGN09634.1};
GN ORFNames=A3C61_01500 {ECO:0000313|EMBL:OGN09634.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_02_FULL_39_10.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802674 {ECO:0000313|EMBL:OGN09634.1, ECO:0000313|Proteomes:UP000178908};
RN [1] {ECO:0000313|EMBL:OGN09634.1, ECO:0000313|Proteomes:UP000178908}
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:OGN09634.1}.
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DR EMBL; MGJO01000017; OGN09634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8F8Z7; -.
DR Proteomes; UP000178908; 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 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 41883 MW; 52ED038FA45B9BC0 CRC64;
MNRKYPIAKP YITSADKKNV MEVLNSGNLS LGPKHKEFEE KFAKKIGTKY ACTVSSGTAG
LHLAMIAAGI KPGDEVITSP FSFIASANCI LYMNAKPVFV DIDPLSYNMD PDKIEAAITP
KTVAILVVHI FGQAADMSKI LKIARKHKLK IIEDSCESIC AEHNGQKVGT FGESAVFAFY
PNKQMTTGEG GMITTNSKKI YKLCSSLRNQ GRAENMQWLD HQYLGYNYRM DELSAAIGIT
QLAKLDKMIK ERQTIAGWYR KYLTPHKQLI QIPETAVNNT HTWFVYVVTL KKPGIRRDEL
ITLLAKQGIS TKPYLPSIHL FSFYKKMFGY KKGDFPISEA VSNSSLALPF YVGLKENDIK
YIVNRLINVI NKSA
//
