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Database: UniProt
Entry: F2JLN8_CELLD
LinkDB: F2JLN8_CELLD
Original site: F2JLN8_CELLD 
ID   F2JLN8_CELLD            Unreviewed;       454 AA.
AC   F2JLN8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ADZ83429.1};
GN   OrderedLocusNames=Clole_1705 {ECO:0000313|EMBL:ADZ83429.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ83429.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ83429.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP002582; ADZ83429.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2JLN8; -.
DR   STRING; 642492.Clole_1705; -.
DR   KEGG; cle:Clole_1705; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_5_0_9; -.
DR   Proteomes; UP000008467; Chromosome.
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; 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   Aminotransferase {ECO:0000313|EMBL:ADZ83429.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Transferase {ECO:0000313|EMBL:ADZ83429.1}.
SQ   SEQUENCE   454 AA;  52308 MW;  BBD79A6050547C9D CRC64;
     MQYDSRLEKS NQIKSKIIEN IREYYEINFK DQQVFTPGER IAYGGRVFDE DEMIHLVDSA
     LEFWLTTGRY SQQFEKEFSE FLSVKYCSLT NSGSSANLLA FMALTSYKLG ERRIQKGDEV
     ITVAAGFPTT IAPIIQYGAI PVFVDVTLPQ YNIDVRQLES AKSERTKAVM VAHTLGNPFD
     IETVKTFCDK YKLWLVEDNC DALGSQYYYK GEWRYTGTIG DIGTSSFYPP HHMTMGEGGA
     VYTNHIELKQ IIESFRDWGR DCFCASGQDN TCKHRFTGQF GELPKGYDHK YVYSHFGYNL
     KVTDMQAAIG CAQLKKLPHF IEERQRNWAY LKKGLADLTA FFLLPEAADK SNPSWFGFLI
     TLKEDVSFSR DDVVQYIESR GIQTRMLFAG NIVRQPCFDE LREAEESYRV VGELLQTDRI
     MKSTFWIGVY PGMTKPMLDY MIQVLHEFVD NNMK
//
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