ID L0HB86_METFS Unreviewed; 878 AA.
AC L0HB86;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Metfor_0958 {ECO:0000313|EMBL:AGB02012.1};
OS Methanoregula formicica (strain DSM 22288 / NBRC 105244 / SMSP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=593750 {ECO:0000313|EMBL:AGB02012.1, ECO:0000313|Proteomes:UP000010824};
RN [1] {ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Imachi H.,
RA Tamaki H., Sekiguchi Y., Kamagata Y., Cadillo-Quiroz H., Zinder S.,
RA Liu W.-T., Woyke T.;
RT "Complete sequence of Methanoregula formicicum SMSP.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB02012.1, ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RX PubMed=25189582;
RA Yamamoto K., Tamaki H., Cadillo-Quiroz H., Imachi H., Kyrpides N.,
RA Woyke T., Goodwin L., Zinder S.H., Kamagata Y., Liu W.T.;
RT "Complete Genome Sequence of Methanoregula formicica SMSPT, a Mesophilic
RT Hydrogenotrophic Methanogen Isolated from a Methanogenic Upflow Anaerobic
RT Sludge Blanket Reactor.";
RL Genome Announc. 2:e00870-14(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 ECO:0000256|RuleBase:RU004504};
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DR EMBL; CP003167; AGB02012.1; -; Genomic_DNA.
DR RefSeq; WP_015284976.1; NC_019943.1.
DR AlphaFoldDB; L0HB86; -.
DR STRING; 593750.Metfor_0958; -.
DR GeneID; 14310271; -.
DR KEGG; mfo:Metfor_0958; -.
DR eggNOG; arCOG00065; Archaea.
DR HOGENOM; CLU_326967_0_0_2; -.
DR InParanoid; L0HB86; -.
DR OrthoDB; 5817at2157; -.
DR Proteomes; UP000010824; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; cd01713; PAPS_reductase; 1.
DR CDD; cd06453; SufS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR002500; PAPS_reduct.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE-RELATED; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AGB02012.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000010824}.
FT DOMAIN 224..386
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT DOMAIN 504..869
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 878 AA; 98709 MW; 6BB000E71E131A08 CRC64;
MLEPPVKKVL YWCDECNVPL VAKSCACGRE GKRIELLQPY ELRPALSADH ALIRRLVQEQ
FGDVPVAKVL LLNKTGGVDR ADLVLMHGER FGWLTFDPVK RSFAFDLAPE VLPFIIRYAT
RGVLDLEAIT DIRKGQGRVG GKRLVLTRPV PNGSVIVKYK GKYGTGVVND GSIKVKELAA
VEPRTRPDPD WDVVIEKNRY HLKNLERNAV RAIKHHITDR PTANISFSGG KDSTAVLHLA
RKAGVTKAFF IDTGLEFPET IAFVKSQGVE IVGGAGDFWQ AVEKAGPPGK DNRWCCKFQK
LRPLKLYLAK VGPCVTIQGN RWYESWNRAS LEETSQNPDN PLQLNVSPIR NWRALEVFLY
LWWQKAEMNP LYEQGIERIG CFLCPAMLES EYEQIRVTHP EYAKRWDDFV ERWAAKKGLP
EEYCQWGLWR WRALPKKMRE LCREKGIAVN EDFTLKQTGP KKRADEMVDI GRERTMKTAM
QEKPTEDLDL TGIRKDFPLV SEVVYFDNAA TSLSPEPVIQ SLVEFERNYR ANVGRGIHRL
TQIASQRYWH AHEKVAEFIG AKGGVTVFTK SSTESINMMA QGFAWKSGDR VLTTVLEHHA
NLLPWYRLKD RGVAVDFADI RDDYTFDLAA FEAAITDRTR LVAITHTSNV LGVITPVQEV
AKICHDHGAL LLVDMAQSVP HMPVDIMALG CDFAAFSGHK MLGPTGTGVL WMKEPVIEPL
LLGGGIVESV TRSGYTLVEG YQRYEAGTGN IAGGIGLGVA VDYLIRLGME RVRRHEQALT
TRVIDGLKKM PRTTVYVPDS PDRRVGVISF TVEGLHPHEV AQRLDEMADI MVRSGHHCCM
PLMDRLGLPN GTVRASLGLY NTIDEVDLFL ATMEEITR
//
