ID B2KBH2_ELUMP Unreviewed; 386 AA.
AC B2KBH2;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU364075};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU364075};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000256|RuleBase:RU364075};
GN OrderedLocusNames=Emin_0437 {ECO:0000313|EMBL:ACC97994.1};
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC97994.1, ECO:0000313|Proteomes:UP000001029};
RN [1] {ECO:0000313|EMBL:ACC97994.1, ECO:0000313|Proteomes:UP000001029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC97994.1,
RC ECO:0000313|Proteomes:UP000001029};
RX PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
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|RuleBase:RU364075};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU364075};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|RuleBase:RU364075}.
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DR EMBL; CP001055; ACC97994.1; -; Genomic_DNA.
DR RefSeq; WP_012414609.1; NC_010644.1.
DR AlphaFoldDB; B2KBH2; -.
DR STRING; 445932.Emin_0437; -.
DR KEGG; emi:Emin_0437; -.
DR HOGENOM; CLU_003433_0_0_0; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000001029; Chromosome.
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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.260.50; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR017772; Cys_deSase_NifS_bac/arc.
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 NCBIfam; TIGR03402; FeS_nifS; 1.
DR PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU364075};
KW Iron-sulfur {ECO:0000256|RuleBase:RU364075};
KW Metal-binding {ECO:0000256|RuleBase:RU364075};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU364075};
KW Reference proteome {ECO:0000313|Proteomes:UP000001029};
KW Transferase {ECO:0000256|RuleBase:RU364075, ECO:0000313|EMBL:ACC97994.1}.
FT DOMAIN 4..363
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 386 AA; 42211 MW; 3E1E13E9CDC80825 CRC64;
MKVIYLDNNA TTRTAPEVVK EMLPYFSEHY GNASSMHTFG GENKKVIEDA RKKMAALIGA
QYPDEIIITA GGTEADNTAI MSAINSFPDK KHIITSAVEH PAVLEVFKNL QAKGYKVDYI
GVDKNGRFNM DEFKAAVNEN TALVSIMWAN SETGTIFPIE EIAKITKEAG SVFHTDAVQA
VGKIPVNVAD TDINMLSFSA HKFHGPKGIG ALYVKRRTRF MPFIIGGHQE KGHRAGTENV
PAIAGFGKAC EMALENLKNT SKTAVLRDRL EKGLLAKISH SKVNGDVENR LPNTSNISFG
YIEGESILLH LNDYGICASS GSACTSGSLE PSHVLRAMCV DFNFAHGSVR FSLSDENTEQ
EIDFVIEKLP PIIETLRQIS PFGRRS
//
