NFS1_PONAB
ID NFS1_PONAB Reviewed; 457 AA.
AC Q5RDE7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cysteine desulfurase, mitochondrial {ECO:0000305};
DE EC=2.8.1.7 {ECO:0000250|UniProtKB:P0A6B9};
DE Flags: Precursor;
GN Name=NFS1 {ECO:0000250|UniProtKB:P0A6B9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-
CC S) clusters. May be involved in the biosynthesis of molybdenum
CC cofactor. {ECO:0000250|UniProtKB:Q9Y697}.
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:0000250|UniProtKB:Q9Y697};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0A6B9};
CC -!- SUBUNIT: Binds ISCU/NIFUN. Forms a complex with LYRM4. Interacts with
CC HSPA9. {ECO:0000250|UniProtKB:Q9Y697}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y697}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9Y697}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=Q5RDE7-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=Q5RDE7-2; Sequence=VSP_021590;
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR EMBL; CR857965; CAH90210.1; -; mRNA.
DR RefSeq; NP_001127252.1; NM_001133780.1. [Q5RDE7-1]
DR AlphaFoldDB; Q5RDE7; -.
DR SMR; Q5RDE7; -.
DR STRING; 9601.ENSPPYP00000012238; -.
DR GeneID; 100174307; -.
DR KEGG; pon:100174307; -.
DR CTD; 9054; -.
DR eggNOG; KOG1549; Eukaryota.
DR InParanoid; Q5RDE7; -.
DR OrthoDB; 664730at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010240; Cys_deSase_IscS.
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 PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02006; IscS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Molybdenum cofactor biosynthesis; Nucleus;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..457
FT /note="Cysteine desulfurase, mitochondrial"
FT /id="PRO_0000260249"
FT ACT_SITE 381
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 127..128
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 235
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 255..257
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 295
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 381
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with ISCU"
FT /note="via persulfide group"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT MOD_RES 258
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_021590"
SQ SEQUENCE 457 AA; 50135 MW; 45F66BDFAC605E2F CRC64;
MLLRAAWRRA AVAVTAAPGP KPAAPTRGLR LRVGDHAPQS AVPADTAAAP EAGPVLRPLY
MDVQATTPLD PRVLDAMLPY LINYYGNPHS RTHAYGWESE AAMERARQQV ASLIGADPRE
IIFTSGATES NNIAIKGVAR FYRSRKKHLI TTQTEHKCVL DSCRSLEAEG FQVTYLPVQK
SGIIDLKELE AAIQPDTSLV SVMTVNNEIG VKQPIAEIGR ICSSRKVYFH TDAAQAVGKI
PLDVNDMKID LMSISGHKIY GPKGVGAIYI RRRPRVRVEA LQSGGGQERG MRSGTVPTPL
VVGLGAACEV AQQEMEYDHK RISKLSERLI QNIMKSLPDV VMNGDPEHHY PGCINLSFAY
VEGESLLMAL KDVALSSGSA CTSASLEPSY VLRAIGTDED LAHSSIRFGV GRFTTEEEVD
YTVEKCIQHV KRLREMSPLW EMVQDGIDLK SIKWTQH
