CYD_SYNE7
ID CYD_SYNE7 Reviewed; 626 AA.
AC Q8KUU5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cysteine desulfurase {ECO:0000303|PubMed:33821786};
DE Short=CyD {ECO:0000303|PubMed:33821786};
DE EC=2.8.1.7 {ECO:0000269|PubMed:33821786};
GN Name=cyd {ECO:0000303|PubMed:33821786}; OrderedLocusNames=Synpcc7942_B2661;
GN ORFNames=anL36;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OG Plasmid pANL.
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of plasmid 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX PubMed=18353436; DOI=10.1016/j.plasmid.2008.01.005;
RA Chen Y., Holtman C.K., Magnuson R.D., Youderian P.A., Golden S.S.;
RT "The complete sequence and functional analysis of pANL, the large plasmid
RT of the unicellular freshwater cyanobacterium Synechococcus elongatus PCC
RT 7942.";
RL Plasmid 59:176-192(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, INDUCTION BY SULFUR STARVATION, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--GLN-225.
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX PubMed=33821786; DOI=10.7554/elife.59288;
RA Nichols R.J., LaFrance B., Phillips N.R., Radford D.R., Oltrogge L.M.,
RA Valentin-Alvarado L.E., Bischoff A.J., Nogales E., Savage D.F.;
RT "Discovery and characterization of a novel family of prokaryotic
RT nanocompartments involved in sulfur metabolism.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Cargo protein of a type 2A encapsulin nanocompartment
CC probably involved in sulfur metabolism. Cysteine desulfurases mobilize
CC the sulfur from L-cysteine to yield L-alanine, an essential step in
CC sulfur metabolism for biosynthesis of a variety of sulfur-containing
CC biomolecules. {ECO:0000269|PubMed:33821786}.
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:33821786};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P77444};
CC -!- ACTIVITY REGULATION: Encapsulated enzyme is 7-fold more active than
CC encapsulated enzyme. {ECO:0000269|PubMed:33821786}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat for encapulated enzyme is 67 sec(-1), for unencapsulated
CC enzyme is 10 sec(-1). {ECO:0000269|PubMed:33821786};
CC -!- SUBUNIT: There are 1-2 copies of this protein in each type 2A
CC encapsulin shell. {ECO:0000269|PubMed:33821786}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:33821786}.
CC -!- INDUCTION: Present in when grown in sulfur-containing media, induced
CC 42-fold after 48 hours of sulfur starvation (at protein level).
CC {ECO:0000269|PubMed:33821786}.
CC -!- DOMAIN: Has a disordered N-terminal domain of about 225 residues that
CC functions as a cargo-loading domain (tested with GFP) and a conserved
CC C-terminal cysteine desulfurase domain. The first 100 residues also
CC function as a cargo-loading domain but not as well as the first 225
CC residues. {ECO:0000269|PubMed:33821786}.
CC -!- DISRUPTION PHENOTYPE: No growth phenotype for a double srpI-cyd
CC deletion mutant in the presence or absence of sulfur.
CC {ECO:0000269|PubMed:33821786}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR EMBL; AF441790; AAM81163.2; -; Genomic_DNA.
DR EMBL; CP000101; ABB58690.1; -; Genomic_DNA.
DR RefSeq; NP_665776.2; NC_004073.2.
DR RefSeq; WP_011055153.1; NC_007595.1.
DR STRING; 1140.Synpcc7942_B2661; -.
DR PRIDE; Q8KUU5; -.
DR EnsemblBacteria; ABB58690; ABB58690; Synpcc7942_B2661.
DR KEGG; syf:Synpcc7942_B2661; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_7_2_3; -.
DR OMA; YLDSACM; -.
DR BioCyc; SYNEL:SYNPCC7942_B2661-MON; -.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:UniProtKB.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR010970; Cys_dSase_SufS.
DR InterPro; 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 SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
PE 1: Evidence at protein level;
KW Encapsulin nanocompartment; Plasmid; Pyridoxal phosphate; Transferase.
FT CHAIN 1..626
FT /note="Cysteine desulfurase"
FT /id="PRO_0000455331"
FT REGION 1..225
FT /note="Cargo-loading domain"
FT /evidence="ECO:0000269|PubMed:33821786"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..626
FT /note="Cysteine desulfurase domain"
FT /evidence="ECO:0000305|PubMed:33821786"
FT ACT_SITE 582
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P77444"
FT MOD_RES 444
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P77444"
FT MUTAGEN 1..225
FT /note="Missing: No longer loaded into nanocompartments, no
FT change in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:33821786"
SQ SEQUENCE 626 AA; 67205 MW; AB4F6510D76A3AF4 CRC64;
MTNTVPSVPA VPNLPTQSDP FFNERSLEQL TQTVLQDLQQ AGVSEAESAP TPLSVPTPAL
PTTSALAVPQ SPTAIANVPA PPSSIDERSL AQLAQAVLQD PQLASAIASI FPSVTLPTSA
SVPRSVPVPP SFLPSLVPTA PPIHDEVGVI PHHQLPVPSQ PTPAGLQQTA SSKSGSGFYF
IDEQVETAIA ALHSNLTVFP QLTTSSIPTL TGAHSAGAVG FDIHQVRRDF PILQERVNGR
PLVWFDNAAT TQKPQVVIDR LSHYYQHENS NIHRAAHELA ARSTDAYEAA REQVRHFLNA
ASTEEVVFVR GTTEAINLVA KSWGSQNLKE GDEIVITWLE HHANIVPWQQ LSAETGARLR
VVPVDDYGQV RLDEYQKLLS DRTKIVSFTQ VSNALGTITP AKEIIELAHR YGAKVLLDGA
QSVSHLAVDV QALDCDWFVF SGHKVFGPTG IGVLYGKQEL LDATLPWQSG GNMIADVTFE
KTVYQPAPAR FEAGTGNIAD AVGLGAALEY VQKIGLEAIA AYEHELLVHG TALLSQIPGL
RLIGTAPHKA AVLSFVLEGF SPEAIGQALN REGIAVRAGH HCAQPILRRF GLETTVRPSL
AFYNTFEELE TLAAAIRRIQ TGSLAL
