ID   A0A0J8D9R0_CLOCY        Unreviewed;       546 AA.
AC   A0A0J8D9R0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=CLCY_1c02830 {ECO:0000313|EMBL:KMT21049.1};
OS   Clostridium cylindrosporum DSM 605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT21049.1, ECO:0000313|Proteomes:UP000036756};
RN   [1] {ECO:0000313|EMBL:KMT21049.1, ECO:0000313|Proteomes:UP000036756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 605 {ECO:0000313|EMBL:KMT21049.1,
RC   ECO:0000313|Proteomes:UP000036756};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT   "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT   HC-1 (DSM 605).";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:KMT21049.1}.
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DR   EMBL; LFVU01000028; KMT21049.1; -; Genomic_DNA.
DR   RefSeq; WP_048571439.1; NZ_LFVU01000028.1.
DR   AlphaFoldDB; A0A0J8D9R0; -.
DR   STRING; 1121307.CLCY_1c02830; -.
DR   PATRIC; fig|1121307.3.peg.648; -.
DR   OrthoDB; 9804407at2; -.
DR   Proteomes; UP000036756; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:KMT21049.1}; Lyase {ECO:0000313|EMBL:KMT21049.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036756};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KMT21049.1}.
FT   DOMAIN          198..519
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   546 AA;  62737 MW;  1E09DC2096A17F6A CRC64;
     MANYTAKRKE LEELYNKISP FELKNKIIAI AESNKNDSAK FLLNAGRGNP NWIADTPRDA
     FFTFGHFATE ECRRVWNEND LAGMPSKDGI AKRLYEYITN HPNAPGIDLL KKIIDYGINV
     EGFNPDEWVY EIADGIIGDN YPLPDRMLIH TEKIVNRYIL QEMYGNKNLN EKLNIFAVEG
     ATAAMCYIFD SLVANSLILK GEKIAIMSPI FTPYLEIPLL SRYDFEIIEI KATETTKDGT
     HTWQYPSSEI EKLKDPSIKA LFIVNPSNPP SVAIRESSIQ EIVNIVENHN PNLIIISDDV
     YCTFVDNFKS ILSYLPHNTI GVYSFSKYFG VTGWRLGVIS LKEDNVIDKT LKSLPQNFKD
     EIIERYESIT TNIDELKFID RLVADSRQVA LNHTAGLSTP QQVQMAFFCG FSLVDKENNY
     KNLTKEICRR RQRLLFENLG LELRKDPLDA SYYTEFDLLE WANHYYGSEF TKYLQANYTP
     VDVLYRLAEE SSIILLSGGG FHGPEWSIRI SLANLNDEDY IKISKELHRI LQDYINSWKS
     YKDGKK
//