ID A0A0P6XP36_9CHLR Unreviewed; 394 AA.
AC A0A0P6XP36;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:KPL77020.1};
GN ORFNames=ADN00_10660 {ECO:0000313|EMBL:KPL77020.1};
OS Ornatilinea apprima.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Ornatilinea.
OX NCBI_TaxID=1134406 {ECO:0000313|EMBL:KPL77020.1, ECO:0000313|Proteomes:UP000050417};
RN [1] {ECO:0000313|EMBL:KPL77020.1, ECO:0000313|Proteomes:UP000050417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3M-1 {ECO:0000313|EMBL:KPL77020.1,
RC ECO:0000313|Proteomes:UP000050417};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Ornatilinea apprima DSM 23815.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPL77020.1}.
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DR EMBL; LGCL01000024; KPL77020.1; -; Genomic_DNA.
DR RefSeq; WP_075062981.1; NZ_LGCL01000024.1.
DR AlphaFoldDB; A0A0P6XP36; -.
DR STRING; 1134406.ADN00_10660; -.
DR PATRIC; fig|1134406.4.peg.2606; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000050417; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050417}.
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 394 AA; 43245 MW; 79A4DD6EDE5DE343 CRC64;
MTHNNSPKIT MSAPDLTDAE RQAVWEVINT PMLSIGPRIQ AFEESFRRYT GCQHAIGVNS
GTSGLHLCVR AAGVGMGDRV ITSPFSFVSS TNVLLFENAV PVFVDVDERT GNLDPVLTAQ
AAADLAEGGA AAQRWLPRRG AEQSGALKAL LAVDVFGQPA DYDLLSPIAR QHNLKLIEDS
CEALGAQYKN RMAGMLGDYG VFAFYPNKQI TTGEGGMIVT NDSAAAELMT ALRNQGRAPG
DTWLSHTYLG YNYRMDEMSA ALGTAQMARI EELLVSRQRV ADLYNQHLAG LPGIEIPYLA
PETTRVSWFV YVIRVARGVD REALAARLAQ RGIPVRPYFL PIHLQPYMVE RFGYREGDFP
ITEDLGRRGL ALPFSGKMDE EQVAYVCQGL RELL
//