ID A1BH69_CHLPD Unreviewed; 385 AA.
AC A1BH69;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Cpha266_1729 {ECO:0000313|EMBL:ABL65746.1};
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL65746.1, ECO:0000313|Proteomes:UP000008701};
RN [1] {ECO:0000313|EMBL:ABL65746.1, ECO:0000313|Proteomes:UP000008701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL65746.1,
RC ECO:0000313|Proteomes:UP000008701};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; CP000492; ABL65746.1; -; Genomic_DNA.
DR RefSeq; WP_011745555.1; NC_008639.1.
DR AlphaFoldDB; A1BH69; -.
DR STRING; 290317.Cpha266_1729; -.
DR KEGG; cph:Cpha266_1729; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_0_10; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000008701; 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; 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; 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 PANTHER; PTHR43807; FI04487P; 1.
DR PANTHER; PTHR43807:SF20; FI04487P; 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:ABL65746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008701};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABL65746.1}.
FT DOMAIN 29..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 385 AA; 42232 MW; 4415413E5A513DDA CRC64;
MTLSLSDRHG CVLQSEIRNM SIECARTGGI NLSQGVCDTP VPASVLQGAR DALTTGINTY
THYAGLPELR RAIALKQNRF SGMNPDPQKE IIVSAGATGA LYCAFQALLN PGDEVIVFEP
FYGYHISTLQ AAEAVPVYLS LKAPDWSFSE HDLESLVTPR TRGIIVNTPA NPSGKVFSLA
ELELVAAFAE RHDLFVFTDE IYEHFLYGGL RHHSFASLPG MQSRTITVSG VSKTFSVTGW
RIGYVIADAK WAQAIGYFND LIYVCAPAPL QAGVAKGLLE LGDEYYRMLS IEYQAKRDRF
CEALSLAGLY PFIPDGAYYV LADVSRLPGT TSKERAMHIL RTTGVAAVPG SAFFQNYAGE
DVVRFCFAKE DSVLKEACQR LKKLR
//
