SOXA_STAND
ID SOXA_STAND Reviewed; 275 AA.
AC D7A6E5; Q7BQR6;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
DE AltName: Full=Cytochrome c551 subunit monoheme {ECO:0000303|PubMed:14645228};
DE AltName: Full=Protein SoxA {ECO:0000312|EMBL:AAR98727.1};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000303|PubMed:14645228, ECO:0000303|PubMed:15848194, ECO:0000303|PubMed:18552405, ECO:0000303|PubMed:21592966};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:18552405};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA {ECO:0000303|PubMed:14645228, ECO:0000303|PubMed:15848194};
DE Short=TOMES protein SoxA {ECO:0000303|PubMed:14645228, ECO:0000303|PubMed:15848194};
DE Flags: Precursor;
GN Name=soxA {ECO:0000312|EMBL:AAR98727.1}; OrderedLocusNames=Snov_0972;
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Starkeya.
OX NCBI_TaxID=639283;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR98727.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-44; 56-64 AND
RP 100-106, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, MASS SPECTROMETRY, EPR SPECTROSCOPY OF THE SOXAX
RP COMPLEX, AND DISULFIDE BOND.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456 {ECO:0000312|EMBL:AAR98727.1};
RX PubMed=14645228; DOI=10.1074/jbc.m310644200;
RA Kappler U., Aguey-Zinsou K.F., Hanson G.R., Bernhardt P.V., McEwan A.G.;
RT "Cytochrome c551 from Starkeya novella: characterization, spectroscopic
RT properties, and phylogeny of a diheme protein of the SoxAX family.";
RL J. Biol. Chem. 279:6252-6260(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 26-32 AND 38-44, FUNCTION, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, CYSTEINE PERSULFIDE AT CYS-236, MASS SPECTROMETRY,
RP EPR SPECTROSCOPY OF THE SOXAX COMPLEX, AND SIGNAL.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456 {ECO:0000269|PubMed:15848194};
RX PubMed=15848194; DOI=10.1016/j.febslet.2005.03.060;
RA Kappler U., Hanson G.R., Jones A., McEwan A.G.;
RT "A recombinant diheme SoxAX cytochrome - implications for the relationship
RT between EPR signals and modified heme-ligands.";
RL FEBS Lett. 579:2491-2498(2005).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP POTENTIOMETRIC TITRATION; EPR SPECTROSCOPY AND MAGNETIC CIRCULAR DICHROISM
RP OF THE SOXAX COMPLEX.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456 {ECO:0000269|PubMed:18552405};
RX PubMed=18552405; DOI=10.1074/jbc.m800315200;
RA Kappler U., Bernhardt P.V., Kilmartin J., Riley M.J., Teschner J.,
RA McKenzie K.J., Hanson G.R.;
RT "SoxAX cytochromes, a new type of heme copper protein involved in bacterial
RT energy generation from sulfur compounds.";
RL J. Biol. Chem. 283:22206-22214(2008).
RN [5] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-236 IN
RP COMPLEXES WITH SOXX AND HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, EPR SPECTROSCOPY OF THE MET-236
RP MUTANT, MAGNETIC CIRCULAR DICHROISM OF THE MUTANT AND WILD-TYPE SOXAX
RP COMPLEXES, ACTIVE SITE, CYSTEINE PERSULFIDE AT CYS-236, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-236.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456 {ECO:0000269|PubMed:21592966};
RX PubMed=21592966; DOI=10.1074/jbc.m110.212183;
RA Kilmartin J.R., Maher M.J., Krusong K., Noble C.J., Hanson G.R.,
RA Bernhardt P.V., Riley M.J., Kappler U.;
RT "Insights into structure and function of the active site of SoxAX
RT cytochromes.";
RL J. Biol. Chem. 286:24872-24881(2011).
CC -!- FUNCTION: C-type monoheme cytochrome, which is part of the SoxAX
CC cytochrome complex involved in sulfur oxidation. The SoxAX complex
CC catalyzes the formation of a heterodisulfide bond between the conserved
CC cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and
CC thiosulfate or other inorganic sulfur substrates. This leads to the
CC liberation of two electrons, which may be transferred from the SoxAX
CC complex to another cytochrome c that then channels them into the
CC respiratory electron transport chain. Some electrons may be used for
CC reductive CO(2) fixation. {ECO:0000269|PubMed:14645228,
CC ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] +
CC thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-
CC cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2;
CC Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY
CC protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-
CC sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689,
CC Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:140664; EC=2.8.5.2;
CC Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194,
CC ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194,
CC ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194,
CC ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
CC Note=Contains a mononuclear Cu(II) center.
CC {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194,
CC ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
CC -!- ACTIVITY REGULATION: Activated by free Cu(II) ions and pH values above
CC 8. {ECO:0000269|PubMed:18552405}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 mM for glutathione (at pH 6.0) {ECO:0000269|PubMed:14645228,
CC ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
CC KM=0.19 mM for glutathione (at pH 7.0) {ECO:0000269|PubMed:14645228,
CC ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966};
CC Vmax=0.124 uM/min/mg enzyme (copper-free) at pH 6.2
CC {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966};
CC Vmax=1.54 uM/min/mg enzyme (copper-loaded) at pH 6.2
CC {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966};
CC Note=kcat is 8.72 sec(-1) and 5.7 sec(-1) for glutathione at pH 6.0
CC and pH 7.0, respectively. {ECO:0000269|PubMed:18552405};
CC Redox potential:
CC E(0) is -479 mV for heme at pH 8.0 (PubMed:21592966). E(0) is -430 mV
CC for heme at pH 6 with copper-loaded SoxAX, -455 mV for heme at pH 7
CC with copper-loaded SoxAX, -486 mV for heme at pH 8 with copper-loaded
CC SoxAX, -424 mV for heme at pH 6 with copper-free SoxAX, -479 mV for
CC heme at pH 7 with copper-free SoxAX, -507 mV for heme at pH 8 with
CC copper-free SoxAX (PubMed:18552405). E(0) is -196 mV for copper
CC center. The Fe (III/II) potentials are +133 mV at pH 6.0, +104 mV at
CC pH 7.0, +49 at pH 7.9 and +10 mV at pH 8.7.
CC {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000269|PubMed:14645228,
CC ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405,
CC ECO:0000269|PubMed:21592966}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15848194,
CC ECO:0000269|PubMed:18552405}.
CC -!- PTM: Cysteine persulfide at Cys-236. {ECO:0000269|PubMed:15848194,
CC ECO:0000269|PubMed:21592966}.
CC -!- MASS SPECTROMETRY: Mass=28687; Mass_error=4; Method=Electrospray;
CC Note=The measured mass is that of mature SoxA with a heme bound and
CC without a cysteine persulfide modification.;
CC Evidence={ECO:0000269|PubMed:15848194};
CC -!- MASS SPECTROMETRY: Mass=28718; Mass_error=4; Method=Electrospray;
CC Note=The measured mass is that of mature SoxA with a heme bound and
CC with a cysteine persulfide modification.;
CC Evidence={ECO:0000269|PubMed:15848194};
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADH88295.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF139113; AAR98727.1; -; Genomic_DNA.
DR EMBL; CP002026; ADH88295.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041782881.1; NC_014217.1.
DR PDB; 3OA8; X-ray; 1.77 A; A/C/E=1-275.
DR PDB; 3OCD; X-ray; 2.25 A; A/C=1-275.
DR PDBsum; 3OA8; -.
DR PDBsum; 3OCD; -.
DR AlphaFoldDB; D7A6E5; -.
DR SMR; D7A6E5; -.
DR STRING; 639283.Snov_0972; -.
DR PRIDE; D7A6E5; -.
DR EnsemblBacteria; ADH88295; ADH88295; Snov_0972.
DR KEGG; sno:Snov_0972; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_079910_0_0_5; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016669; F:oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0016783; F:sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0019417; P:sulfur oxidation; IDA:UniProtKB.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR025710; SoxA.
DR PIRSF; PIRSF038455; SoxA; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR TIGRFAMs; TIGR04484; thiosulf_SoxA; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transferase; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:15848194"
FT CHAIN 26..275
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_5000603848"
FT DOMAIN 163..263
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 236
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:21592966"
FT BINDING 183
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:21592966"
FT BINDING 187
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:21592966"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 236
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:21592966"
FT DISULFID 74..110
FT /evidence="ECO:0000269|PubMed:14645228,
FT ECO:0000269|PubMed:21592966"
FT MUTAGEN 236
FT /note="C->M: 564 mV change in redox potential of the heme.
FT Catalytically active, but 46% reduction in turnover number
FT in an enzyme assay that uses reduced glutathione as the
FT sulfur substrate. Also active in SoxYZ-based enzyme assay
FT using thiosulfate as the sulfur substrate with 30%
FT reduction in the activity compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:21592966"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:3OA8"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3OA8"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3OA8"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:3OA8"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:3OA8"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:3OA8"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:3OA8"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3OA8"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3OA8"
SQ SEQUENCE 275 AA; 30684 MW; 5F9322D234CCC3CF CRC64;
MRRFAAGCLA LALLVLPFVL TGARAAEDES EKEIERYRQM IEDPMANPGF LNVDRGEVLW
SEPRGTRNVS LETCDLGEGP GKLEGAYAHL PRYFADTGKV MDLEQRLLWC METIQGRDTK
PLVAKPFSGP GRTSDMEDLV AFIANKSDGV KIKVALATPQ EKEMYAIGEA LFFRRSSIND
FSCSTCHGAA GKRIRLQALP QLDVPGKDAQ LTMATWPTYR VSQSALRTMQ HRMWDCYRQM
RMPAPDYASE AVTALTLYLT KQAEGGELKV PSIKR
