SUFS_BACSU
ID SUFS_BACSU Reviewed; 406 AA.
AC O32164;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cysteine desulfurase SufS;
DE EC=2.8.1.7 {ECO:0000269|PubMed:27382962};
GN Name=sufS; Synonyms=csd, yurW; OrderedLocusNames=BSU32690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, REACTION MECHANISM, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF CYS-361.
RC STRAIN=168 / PS832;
RX PubMed=20822158; DOI=10.1021/bi101358k;
RA Selbach B., Earles E., Dos Santos P.C.;
RT "Kinetic analysis of the bisubstrate cysteine desulfurase SufS from
RT Bacillus subtilis.";
RL Biochemistry 49:8794-8802(2010).
RN [3]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=20097860; DOI=10.1128/jb.01536-09;
RA Albrecht A.G., Netz D.J., Miethke M., Pierik A.J., Burghaus O.,
RA Peuckert F., Lill R., Marahiel M.A.;
RT "SufU is an essential iron-sulfur cluster scaffold protein in Bacillus
RT subtilis.";
RL J. Bacteriol. 192:1643-1651(2010).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=21744456; DOI=10.1002/cbic.201100190;
RA Albrecht A.G., Landmann H., Nette D., Burghaus O., Peuckert F., Seubert A.,
RA Miethke M., Marahiel M.A.;
RT "The frataxin homologue Fra plays a key role in intracellular iron
RT channeling in Bacillus subtilis.";
RL ChemBioChem 12:2052-2061(2011).
RN [5]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH SUFU,
RP AND SUBUNIT.
RC STRAIN=168;
RX PubMed=21236255; DOI=10.1016/j.febslet.2011.01.005;
RA Albrecht A.G., Peuckert F., Landmann H., Miethke M., Seubert A.,
RA Marahiel M.A.;
RT "Mechanistic characterization of sulfur transfer from cysteine desulfurase
RT SufS to the iron-sulfur scaffold SufU in Bacillus subtilis.";
RL FEBS Lett. 585:465-470(2011).
RN [6]
RP REACTION MECHANISM, AND ACTIVITY REGULATION.
RC STRAIN=168 / PS832;
RX PubMed=24321018; DOI=10.1021/bi4011978;
RA Selbach B.P., Chung A.H., Scott A.D., George S.J., Cramer S.P.,
RA Dos Santos P.C.;
RT "Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-
RT dependent sulfur transfer protein.";
RL Biochemistry 53:152-160(2014).
RN [7] {ECO:0007744|PDB:5J8Q}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), SUBUNIT, INTERACTION WITH SUFU AND
RP FRA, ACTIVE SITE, AND CATALYTIC ACTIVITY.
RC STRAIN=168;
RX PubMed=27382962; DOI=10.1371/journal.pone.0158749;
RA Blauenburg B., Mielcarek A., Altegoer F., Fage C.D., Linne U., Bange G.,
RA Marahiel M.A.;
RT "Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its
RT Dynamic Interaction with Frataxin and Scaffold Protein SufU.";
RL PLoS ONE 11:e0158749-e0158749(2016).
RN [8] {ECO:0007744|PDB:5XT5, ECO:0007744|PDB:5XT6}
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS), FUNCTION, AND INTERACTION WITH
RP SUFU.
RC STRAIN=168;
RX PubMed=29235855; DOI=10.1021/jacs.7b11307;
RA Fujishiro T., Terahata T., Kunichika K., Yokoyama N., Maruyama C., Asai K.,
RA Takahashi Y.;
RT "Zinc-Ligand Swapping Mediated Complex Formation and Sulfur Transfer
RT between SufS and SufU for Iron-Sulfur Cluster Biogenesis in Bacillus
RT subtilis.";
RL J. Am. Chem. Soc. 139:18464-18467(2017).
RN [9] {ECO:0007744|PDB:5ZS9, ECO:0007744|PDB:5ZSK, ECO:0007744|PDB:5ZSO, ECO:0007744|PDB:6KFZ}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS), FUNCTION, AND ACTIVE SITE.
RX PubMed=31587510; DOI=10.1111/febs.15081;
RA Nakamura R., Hikita M., Ogawa S., Takahashi Y., Fujishiro T.;
RT "Snapshots of PLP-substrate and PLP-product external aldimines as
RT intermediates in two types of cysteine desulfurase enzymes.";
RL FEBS J. 287:1138-1154(2020).
CC -!- FUNCTION: Type II cysteine desulfurase that acts as the initial step in
CC the SUF-like Fe-S cluster assembly pathway. Catalyzes the removal of
CC elemental sulfur atoms from L-cysteine by using the cofactor pyridoxal
CC 5'-phosphate (PLP), resulting in the production of L-alanine and
CC persulfide (PubMed:31587510). Activity is stimulated by SufU, which
CC acts as a sulfurtransferase that receives sulfur from SufS via a zinc-
CC ligand swapping mechanism and transfers it to SufB (PubMed:29235855,
CC PubMed:27382962). {ECO:0000269|PubMed:20097860,
CC ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21744456,
CC ECO:0000269|PubMed:27382962, ECO:0000269|PubMed:29235855,
CC ECO:0000269|PubMed:31587510}.
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; Evidence={ECO:0000269|PubMed:20822158,
CC ECO:0000269|PubMed:27382962};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: A Cys to Ala mutation in SufU (Cys-41-Ala) has
CC been described to be a competivie inhibitor of SufS activity and a non-
CC competitive inhibitor (PubMed:21236255, PubMed:24321018).
CC {ECO:0000269|PubMed:21236255, ECO:0000269|PubMed:24321018}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=86 uM for L-cysteine {ECO:0000269|PubMed:20822158,
CC ECO:0000269|PubMed:21236255};
CC KM=30 uM for SufU {ECO:0000269|PubMed:20822158,
CC ECO:0000269|PubMed:21236255};
CC Vmax=1157 nmol/min/mg enzyme in the presence of SufU
CC {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255};
CC Note=In the presence of dithiothreitol, which regenerates the second
CC reaction product SufU.S.;
CC -!- SUBUNIT: Homodimer (PubMed:27382962). Interacts with SufU; this
CC interaction induces an opening of the active site pocket of SufS
CC (PubMed:27382962). Interacts with frataxin/Fra (PubMed:27382962).
CC {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255,
CC ECO:0000269|PubMed:27382962}.
CC -!- INTERACTION:
CC O32164; O32163: sufU; NbExp=8; IntAct=EBI-7826704, EBI-8561343;
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB15258.1; -; Genomic_DNA.
DR PIR; F70019; F70019.
DR RefSeq; NP_391148.1; NC_000964.3.
DR RefSeq; WP_003228604.1; NZ_JNCM01000033.1.
DR PDB; 5J8Q; X-ray; 1.70 A; A=1-406.
DR PDB; 5XT5; X-ray; 2.34 A; A/B=1-406.
DR PDB; 5XT6; X-ray; 3.50 A; A/B=1-406.
DR PDB; 5ZS9; X-ray; 2.80 A; A=1-406.
DR PDB; 5ZSK; X-ray; 3.24 A; A=1-406.
DR PDB; 5ZSO; X-ray; 2.70 A; A=1-406.
DR PDB; 6KFY; X-ray; 1.97 A; A=1-406.
DR PDB; 6KFZ; X-ray; 1.96 A; A=1-406.
DR PDB; 7CEO; X-ray; 2.43 A; A=1-406.
DR PDB; 7CEP; X-ray; 2.05 A; A=1-406.
DR PDB; 7CEQ; X-ray; 2.00 A; A=1-406.
DR PDB; 7CER; X-ray; 2.30 A; A=1-406.
DR PDB; 7CES; X-ray; 2.20 A; A=1-406.
DR PDB; 7E6A; X-ray; 1.96 A; A=1-406.
DR PDB; 7E6B; X-ray; 1.84 A; A=1-406.
DR PDB; 7E6C; X-ray; 1.73 A; A=1-406.
DR PDB; 7E6D; X-ray; 2.67 A; A=1-406.
DR PDB; 7E6E; X-ray; 2.28 A; A=1-406.
DR PDB; 7E6F; X-ray; 2.74 A; A=1-406.
DR PDBsum; 5J8Q; -.
DR PDBsum; 5XT5; -.
DR PDBsum; 5XT6; -.
DR PDBsum; 5ZS9; -.
DR PDBsum; 5ZSK; -.
DR PDBsum; 5ZSO; -.
DR PDBsum; 6KFY; -.
DR PDBsum; 6KFZ; -.
DR PDBsum; 7CEO; -.
DR PDBsum; 7CEP; -.
DR PDBsum; 7CEQ; -.
DR PDBsum; 7CER; -.
DR PDBsum; 7CES; -.
DR PDBsum; 7E6A; -.
DR PDBsum; 7E6B; -.
DR PDBsum; 7E6C; -.
DR PDBsum; 7E6D; -.
DR PDBsum; 7E6E; -.
DR PDBsum; 7E6F; -.
DR AlphaFoldDB; O32164; -.
DR SMR; O32164; -.
DR IntAct; O32164; 2.
DR MINT; O32164; -.
DR STRING; 224308.BSU32690; -.
DR jPOST; O32164; -.
DR PaxDb; O32164; -.
DR PRIDE; O32164; -.
DR EnsemblBacteria; CAB15258; CAB15258; BSU_32690.
DR GeneID; 937108; -.
DR KEGG; bsu:BSU32690; -.
DR PATRIC; fig|224308.179.peg.3540; -.
DR eggNOG; COG0520; Bacteria.
DR InParanoid; O32164; -.
DR OMA; HKLCGPT; -.
DR PhylomeDB; O32164; -.
DR BioCyc; BSUB:BSU32690-MON; -.
DR BRENDA; 2.8.1.7; 658.
DR Proteomes; UP000001570; 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="Cysteine desulfurase SufS"
FT /id="PRO_0000150293"
FT ACT_SITE 361
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:27382962,
FT ECO:0000269|PubMed:31587510"
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:31587510,
FT ECO:0007744|PDB:5J8Q"
FT MUTAGEN 361
FT /note="C->A: Loss of cysteine desulfurase activity, still
FT binds SufU and Cys."
FT /evidence="ECO:0000269|PubMed:20822158"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:7CEP"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 58..78
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:5J8Q"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5J8Q"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 296..315
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:5J8Q"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5J8Q"
FT HELIX 385..406
FT /evidence="ECO:0007829|PDB:5J8Q"
SQ SEQUENCE 406 AA; 44922 MW; E433C0B5965349D1 CRC64;
MNITDIREQF PILHQQVNGH DLVYLDSAAT SQKPRAVIET LDKYYNQYNS NVHRGVHTLG
TRATDGYEGA REKVRKFINA KSMAEIIFTK GTTTSLNMVA LSYARANLKP GDEVVITYME
HHANIIPWQQ AVKATGATLK YIPLQEDGTI SLEDVRETVT SNTKIVAVSH VSNVLGTVNP
IKEMAKIAHD NGAVIVVDGA QSTPHMKIDV QDLDCDFFAL SSHKMCGPTG VGVLYGKKAL
LENMEPAEFG GEMIDFVGLY ESTWKELPWK FEAGTPIIAG AIGLGAAIDF LEEIGLDEIS
RHEHKLAAYA LERFRQLDGV TVYGPEERAG LVTFNLDDVH PHDVATVLDA EGIAVRAGHH
CAQPLMKWLD VTATARASFY LYNTEEEIDK LVEALQKTKE YFTNVF
