SUFS_HALVD
ID SUFS_HALVD Reviewed; 424 AA.
AC D4GYV5; D2ECC4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Cysteine desulfurase;
DE EC=2.8.1.7;
DE AltName: Full=Selenocysteine lyase;
DE EC=4.4.1.16;
GN Name=sufS; OrderedLocusNames=HVO_0109; ORFNames=C498_18783;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=DS2;
RX PubMed=20226884; DOI=10.1016/j.bbapap.2010.03.001;
RA Zafrilla B., Martinez-Espinosa R.M., Esclapez J., Perez-Pomares F.,
RA Bonete M.J.;
RT "SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in
RT haloarchaea.";
RL Biochim. Biophys. Acta 1804:1476-1482(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC to produce alanine. Able to reassemble a removed [2Fe-2S] cluster of an
CC apo-ferredoxin. Shows a selenocysteine lyase activity approximately
CC 280-fold higher than its cysteine desulfurase activity.
CC {ECO:0000269|PubMed:20226884}.
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:0000269|PubMed:20226884};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC ChEBI:CHEBI:57972; EC=4.4.1.16;
CC Evidence={ECO:0000269|PubMed:20226884};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20226884};
CC -!- ACTIVITY REGULATION: DTT increases activity up to 46%, but has an
CC inhibitory effect at concentrations higher than 5 mM in vitro.
CC {ECO:0000269|PubMed:20226884}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.032 mM for L-cysteine {ECO:0000269|PubMed:20226884};
CC KM=0.97 mM for L-selenocysteine {ECO:0000269|PubMed:20226884};
CC Vmax=0.051 umol/min/mg enzyme with L-cysteine as substrate
CC {ECO:0000269|PubMed:20226884};
CC Vmax=11.8 umol/min/mg enzyme with L-selenocysteine as substrate
CC {ECO:0000269|PubMed:20226884};
CC pH dependence:
CC Optimum pH is 7.5. Remains partially active at pH 11.
CC {ECO:0000269|PubMed:20226884};
CC Temperature dependence:
CC Optimum temperature is 55-60 degrees Celsius in the presence of 0-0.5
CC M KCl and 70-75 degrees Celsius in the presence of 2.5-3.0 M KCl.
CC {ECO:0000269|PubMed:20226884};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20226884}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBI67620.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN598908; CBI67620.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001956; ADE05148.1; -; Genomic_DNA.
DR EMBL; AOHU01000105; ELY24323.1; -; Genomic_DNA.
DR RefSeq; WP_049914909.1; NZ_AOHU01000105.1.
DR AlphaFoldDB; D4GYV5; -.
DR SMR; D4GYV5; -.
DR STRING; 309800.C498_18783; -.
DR EnsemblBacteria; ADE05148; ADE05148; HVO_0109.
DR EnsemblBacteria; ELY24323; ELY24323; C498_18783.
DR GeneID; 8924530; -.
DR KEGG; hvo:HVO_0109; -.
DR PATRIC; fig|309800.29.peg.3658; -.
DR eggNOG; arCOG00065; Archaea.
DR HOGENOM; CLU_003433_2_5_2; -.
DR OMA; HKLCGPT; -.
DR OrthoDB; 24071at2157; -.
DR BRENDA; 2.8.1.7; 2561.
DR BRENDA; 4.4.1.16; 2561.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009000; F:selenocysteine lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR CDD; cd06453; SufS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
PE 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="Cysteine desulfurase"
FT /id="PRO_0000428944"
FT ACT_SITE 382
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 46552 MW; 785FC7FCBADE8FB2 CRC64;
MQESYPVDVD AIRADFPILE RKVGGDISTP GEHDDDTTPL VYLDNAATSH TPEQVVDAIV
DYYHGYNSNV HRGIHHLSQE ASVAYEDAHD RVAEFIGASG GREEVVFTKN TTESMNLVAY
AWGLDELGPG DSVVMTEMEH HASLVTWQQI AKKTGAEVRY IRVDDDGRLD MEHAKELIDD
STKMVSVVHV SNTLGTVNPV SELADMAHEV GSYIFVDGAQ SVPTRPVDVE DIDADFFAFS
GHKMCGPTGI GALYGKRDIL DEMGPYLYGG EMIRSVTYED STWEDLPWKF EAGTPPIAQG
VGFAAAVDYL DDIGMENVQA HEELLAEYAY DRLTEFDDIE IYGPPGDDRG GLVSFNLDSV
HAHDLSSILN EQGVAIRAGD HCTQPLHDKL GVAASTRASF YIYNAREEVD KLVDAIDAAR
ELFA
