GenomeNet

Database: UniProt
Entry: F0T7T7_METLA
LinkDB: F0T7T7_METLA
Original site: F0T7T7_METLA 
ID   F0T7T7_METLA            Unreviewed;       402 AA.
AC   F0T7T7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   OrderedLocusNames=Metbo_0172 {ECO:0000313|EMBL:ADZ08424.1};
OS   Methanobacterium lacus (strain AL-21).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=877455 {ECO:0000313|EMBL:ADZ08424.1, ECO:0000313|Proteomes:UP000007490};
RN   [1] {ECO:0000313|Proteomes:UP000007490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL-21 {ECO:0000313|Proteomes:UP000007490};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Cadillo-Quiroz H.,
RA   Imachi H., Zinder S., Liu W., Woyke T.;
RT   "Complete sequence of Methanobacterium sp. AL-21.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADZ08424.1, ECO:0000313|Proteomes:UP000007490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL-21 {ECO:0000313|EMBL:ADZ08424.1,
RC   ECO:0000313|Proteomes:UP000007490};
RX   PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA   Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT   "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT   lacus isolated from northern peatlands.";
RL   Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001357};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
CC       {ECO:0000256|ARBA:ARBA00010447}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002551; ADZ08424.1; -; Genomic_DNA.
DR   RefSeq; WP_013643775.1; NC_015216.1.
DR   AlphaFoldDB; F0T7T7; -.
DR   STRING; 877455.Metbo_0172; -.
DR   GeneID; 10276598; -.
DR   KEGG; mel:Metbo_0172; -.
DR   eggNOG; arCOG00065; Archaea.
DR   HOGENOM; CLU_003433_2_4_2; -.
DR   OrthoDB; 5817at2157; -.
DR   Proteomes; UP000007490; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE-RELATED; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007490};
KW   Transferase {ECO:0000313|EMBL:ADZ08424.1}.
FT   DOMAIN          20..389
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   402 AA;  43938 MW;  E74E7C8E417AEA19 CRC64;
     MENGVDINIR ADIPLLEDVI YLDAASTTPT PKPVVESMCN YFYNYNTNTG RGAYNLAVRA
     TKEFESSRKR ISKFVGSKPS EIIFTKNTTE AINLVANGLN FKKGDSVVVP NIEHHSNFVP
     WLNLRKKGVN LKLVEADEYG IIDHSDVLDA VDANTKLITT THVSNAIGSV QPIKEIGEIA
     DENDVLYLVD AAQSAGHMPL DVKDIKADFV SVPGHKGLLG PIGTGFLYCN QEISEDLEPT
     NYGGGTVLDV TESDFTLETV PARFEGGTQN IAGVIGLGTA VDYLERIGME KIQNHSKKLT
     AKLFKEVNDI ENTIVYGSPE NIYGIVAFNI DGVNAHDVAK ILDEVKGICV RSGHHCAIPA
     IRHMGAYELG GTVRASVHYY NTVEEIEIFG ETLREISKFF GD
//
DBGET integrated database retrieval system