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Database: UniProt
Entry: A0A398CLL1_9BACL
LinkDB: A0A398CLL1_9BACL
Original site: A0A398CLL1_9BACL 
ID   A0A398CLL1_9BACL        Unreviewed;       401 AA.
AC   A0A398CLL1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:RIE03140.1};
DE            EC=2.6.1.92 {ECO:0000313|EMBL:RIE03140.1};
GN   Name=pseC {ECO:0000313|EMBL:RIE03140.1};
GN   ORFNames=D3H35_15045 {ECO:0000313|EMBL:RIE03140.1};
OS   Cohnella faecalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2315694 {ECO:0000313|EMBL:RIE03140.1, ECO:0000313|Proteomes:UP000266340};
RN   [1] {ECO:0000313|EMBL:RIE03140.1, ECO:0000313|Proteomes:UP000266340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2E09-144 {ECO:0000313|EMBL:RIE03140.1,
RC   ECO:0000313|Proteomes:UP000266340};
RA   Zhu H.;
RT   "Cohnella cavernae sp. nov., isolated from a karst cave.";
RL   Submitted (SEP-2018) 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:RIE03140.1}.
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DR   EMBL; QXJM01000039; RIE03140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398CLL1; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000266340; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   Aminotransferase {ECO:0000313|EMBL:RIE03140.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266340};
KW   Transferase {ECO:0000313|EMBL:RIE03140.1}.
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         200
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   401 AA;  43941 MW;  681443AFF50252E8 CRC64;
     MDQQVGFDSF ALGGSEMREK MLPYGCQQID DDDVAAVVDI LRSAWLTQGP AIERFERDIA
     DYSGAKHAVA FANGTAALHG ACYAAGIGQG DEVITSPLTF VASSNCVLYC GGKPVFADIR
     PDTYNLDPQA VLEQITDKTK AIIPVDFSGQ PAEMDAFSAI ARDHGLVVIE DAAHSLGAEY
     GGRRTGSLAD MTMFSFHPVK HITTGEGGII VTDSAEYADR LRAFRSHGIT RDPGQLLRND
     GPWYYEMQSL GYNYRITDLQ AALGSSQLKK LDTFVARRRE IAAAYTGALA GVPGLQVPYQ
     HPDTNSSWHL YVLRWKKDIL PGGRDRAFDI LRSLNIGVHV HYIPVYQQPY YQSIGYETTV
     CSHAEAYYSE ALSLPIFPGM TDRDVQDVID AVLETVNLLA I
//
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