ID A3QIC2_SHELP Unreviewed; 759 AA.
AC A3QIC2;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000256|ARBA:ARBA00031911};
GN OrderedLocusNames=Shew_3354 {ECO:0000313|EMBL:ABO25220.1};
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO25220.1, ECO:0000313|Proteomes:UP000001558};
RN [1] {ECO:0000313|EMBL:ABO25220.1, ECO:0000313|Proteomes:UP000001558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC to produce alanine. Seems to participate in the biosynthesis of the
CC nitrogenase metalloclusters by providing the inorganic sulfur required
CC for the Fe-S core formation. {ECO:0000256|ARBA:ARBA00003120}.
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};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; CP000606; ABO25220.1; -; Genomic_DNA.
DR RefSeq; WP_011867150.1; NC_009092.1.
DR AlphaFoldDB; A3QIC2; -.
DR STRING; 323850.Shew_3354; -.
DR KEGG; slo:Shew_3354; -.
DR eggNOG; COG0491; Bacteria.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_6; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000001558; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 1.10.260.50; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABO25220.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001558};
KW Transferase {ECO:0000313|EMBL:ABO25220.1}.
FT DOMAIN 671..758
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 759 AA; 82038 MW; B71095AD1124FD0D CRC64;
MHHTSPLSQI YLDANATTPV LPQAAKAALG AMEDLFGNPS SSHITGLKAK SLMEQTRLRA
KQILGSGQGN IIFTSGATEG IQTAILSALI KAKASLDPNK QYSLLYGATE HKAVPNSLAH
WNQLLEIGAE LKAIPVDDKG ALDLDFIAAE VPNALMICTM AVNNETGVYQ DLKALDTCIR
DHNPEVFWMV DCVQALGKRP LALAQTSIDY APFSGHKLYA PKGIGFVYIR DGAPFTPFIA
GGGQEGGLRS GTENLPGMAA LNQVFAMLLA EQDSAFHSLS TLVDYREQLA QALKRAFPTL
VFNHSFDNSV PTTLNFAVPG FSSKEIMDLF DAANIRVSSG SACSSKVTRS FVLDAMGLPA
WQSESAIRLS FGPAMTQTEV DQACERIQSA ANALGNSCLT LSSGEASADK QPLNGLVQLK
SGSSCSWIYA DQESKQAVVI DPLPELDQRI DTLLQCQQLE PIAFIDTHGH ADHVSGRVAL
AARYLPEQTS DHLGWPEDHQ ITEIGARPAQ AISLGQYSLV KLATPGHTND SISLLLCSPQ
GEVSYAFCGD LVLMGSLGRT NFDSSCAKQM YNSLKLLHSL IGDDTLLCPS HDYNNEFTTS
FAAEFRVNPL LNEVINGTIS MAQFELQKAR LDTHLKDEAG SEIICGAYTG GCSKAKVKEY
DSQSLQLQVS QSPQLKLLDI REPHEYALQH ELGTLSEQTI NVPMTRLVQF VQEHKQESDA
EWVLVCRSGS RSLVAAQALH RLGFNKIAHL KGGYALSDS
//
