ID A0LUT7_ACIC1 Unreviewed; 400 AA.
AC A0LUT7;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent enzyme {ECO:0000313|EMBL:ABK53197.1};
GN OrderedLocusNames=Acel_1425 {ECO:0000313|EMBL:ABK53197.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53197.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK53197.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP000481; ABK53197.1; -; Genomic_DNA.
DR RefSeq; WP_011720260.1; NC_008578.1.
DR AlphaFoldDB; A0LUT7; -.
DR STRING; 351607.Acel_1425; -.
DR KEGG; ace:Acel_1425; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_2_11; -.
DR InParanoid; A0LUT7; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 400 AA; 42221 MW; E18E7BE4E46D2002 CRC64;
MNDAGTPRHP EQSDPRCQSA EPADTGRSGA TPIVSGDGTR VLTAGGMPGG QGTPLVPSPV
FASTYVLHGE PAGPYQYGRL TNPTWTAWEA ALADLEGGPA IAFASGIAAV TAVLATTLRP
GDTMLMASDC YYATRRLAEE FLSDFGVVTR WAPTGPEMAA QVAGARLVWI ESPSNPGLDV
CDIAELARRC RDEGALLAVD NTTATPLGQQ PLLLGADFSV ASDTKAMTGH SDIVLGHVAC
RTGELAERIR GWRNSTGAIP GPFETWLAHR SLATLDLRLA RQADNARELA AMLAAHPAVR
RVRYPWLPSD PAYPLAVRQM RRPGGLVSFE LAGAAEAEAF LGALRLVTVA TSFGGVHSTA
ERRARWGGDD VPPGFIRFSC GCEDAADLLA DVEQALARLR
//
