ID K0NNR7_DESTT Unreviewed; 492 AA.
AC K0NNR7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Cystathione beta-synthase modulated DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:CCK81693.1};
GN OrderedLocusNames=TOL2_C35360 {ECO:0000313|EMBL:CCK81693.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK81693.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK81693.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FO203503; CCK81693.1; -; Genomic_DNA.
DR AlphaFoldDB; K0NNR7; -.
DR STRING; 651182.TOL2_C35360; -.
DR KEGG; dto:TOL2_C35360; -.
DR PATRIC; fig|651182.5.peg.4159; -.
DR HOGENOM; CLU_033332_2_3_7; -.
DR OrthoDB; 9771070at2; -.
DR Proteomes; UP000007347; 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; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51371; CBS; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CCK81693.1};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000313|EMBL:CCK81693.1}.
FT DOMAIN 9..67
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 492 AA; 54606 MW; 62FDC2B147829F44 CRC64;
MQGHFTYLKE RIEDISARED TSIRKVLKQI DKGALGIALL VEPDTGIFKG ILTDGDVRRA
LILGLELDSA VSNIVRPKSI TASIDTSSEQ LSKLFGEAVR IIPLLDKHNK VVDLALFDTR
IYLPVSEPNL GEKELKYVSD CILTGWVSSA GKYVTRFEQM FAKFCGTKFG ISSSSGTTAL
HLSLLALGIG AGDEVIVPSF TFISTANAVA FTGANPVFVD SEMETWNIDP QKIEQAITSR
TKAIIPVHIY GHPAQMSSIL EIAGKYNLAV VEDAAEAHGA LYKGNKTGSL GDMGIFSFYG
NKIITTGEGG MVVTDNKELA DKIRIFRDHG MDTEKRYRHS VLGYNYRMTN IQAALGVGQM
ERIDQIIEQK CTNAFLYSKE LKNIPGITLP PNEKWAKNIY WLYSILIDEK KFGMSSVELG
KRLKIKSIET RPLFPPVHQQ PIYDTKQNLP VCEKLSNSGL SLPSSTNIKK DEINRIAWEI
KKIKNQTTNE MF
//
