ID A5N621_CLOK5 Unreviewed; 543 AA.
AC A5N621;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Predicted aminotransferase {ECO:0000313|EMBL:EDK32752.1};
GN OrderedLocusNames=CKL_0699 {ECO:0000313|EMBL:EDK32752.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32752.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK32752.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP000673; EDK32752.1; -; Genomic_DNA.
DR RefSeq; WP_011989267.1; NC_009706.1.
DR AlphaFoldDB; A5N621; -.
DR STRING; 431943.CKL_0699; -.
DR KEGG; ckl:CKL_0699; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_038911_0_0_9; -.
DR Proteomes; UP000002411; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 1.10.20.110; -; 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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR022518; Aspartate_4-decarboxylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03801; asp_4_decarbox; 1.
DR PANTHER; PTHR43795:SF10; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EDK32752.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000002411};
KW Transferase {ECO:0000313|EMBL:EDK32752.1}.
FT DOMAIN 200..520
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 543 AA; 62817 MW; A80C8EF4C6B6A0B6 CRC64;
MYNKNIQLLE LERIYGRISP FELKDKLINL AKNQKKKSVR TLLDAGRGNP NWVAITPREA
FFTFGQFAAE ECRRTWNQDT LAGMPQKKGI DKRFYTYLED HKNSPGVELL KNIINYGINF
QGFIAEDWIY ELTDGIIGDN YPTPNRMLIH VEKIVHQYLI ERIYNIKDSS LEFKLFSVEG
ATAAICYIFD SLIANELLHR RDKIAIMTPI FTPYLEIPVI PRYDFDLIRI MASESLEDST
HTWQYPKSEL EKLYDPGIKA LFLVNPSNPP SVAIRSESIE YLVKIVKNKN PNLMIISDDV
YGTFPDNFHS IVSALPFNSI GVYSFSKYFR VTGWRLGTIA LHKNNIFDKL LKALPENKKK
SIKKRYEALS VNPGEIDFID RIVADSRQVA LQHTAGLSTP QQVQMAFFAA FDLLDKEKKY
RNLTNSICRK RKKLLFDGLG IDLQKNEYDA SYYAEFDLLE WSEHHYGKEF GSYLKENYKP
VDILFKLAEK SSIVLLSGAG FYAPEWSIRI SLANLNDESY SEIGHILHNI LKDCLRDWKN
SRK
//
