GenomeNet

Database: UniProt
Entry: Q8TU38_METAC
LinkDB: Q8TU38_METAC
Original site: Q8TU38_METAC 
ID   Q8TU38_METAC            Unreviewed;       393 AA.
AC   Q8TU38;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   OrderedLocusNames=MA_0236 {ECO:0000313|EMBL:AAM03689.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM03689.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM03689.1, ECO:0000313|Proteomes:UP000002487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000313|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA   Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA   Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA   de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA   Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA   Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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         ECO:0000256|RuleBase:RU004504};
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; AE010299; AAM03689.1; -; Genomic_DNA.
DR   RefSeq; WP_011020294.1; NC_003552.1.
DR   AlphaFoldDB; Q8TU38; -.
DR   STRING; 188937.MA_0236; -.
DR   EnsemblBacteria; AAM03689; AAM03689; MA_0236.
DR   GeneID; 1472128; -.
DR   KEGG; mac:MA_0236; -.
DR   HOGENOM; CLU_003433_2_5_2; -.
DR   InParanoid; Q8TU38; -.
DR   OrthoDB; 5817at2157; -.
DR   PhylomeDB; Q8TU38; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT   DOMAIN          18..381
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   393 AA;  43050 MW;  26CF0835326B54AF CRC64;
     MYDVYAVRED FPVLKEVVYL DSTATTQTPI PAVEAMVEYF YKYAGNHGRG AHRLARETTN
     RYEDARETVA RFLNSEPSKT VFTKNTTEGI NFVANSYPWE AGDHIVTTLL EHHSNLLPWL
     RLQKKGVNVT VVSPDRKGII DPQVIENALT DRTKLIAVTH ISNVFGSVQD VIRITKLAHR
     NEVKVLIDGA QSAGHIPVDL KTLGCDFFAT AGHKGLLGPQ GTGVLYIKQP EVLESASVGG
     GTVSGVKGLA YTLEPSPACF EAGTPNIPGV IGLGRAVEYV EKIGVSEIKK HEEKLSREAA
     KRLSEFEHVE VYGPENRAGI VPFNVKGLHA HDVALILDQT KKICIRSGHH CAIPVTRFLE
     VESTARASFA LYNTEEEVDI FVNAVDALKA LVS
//
DBGET integrated database retrieval system