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Database: UniProt
Entry: A0A0C5VBX4_9GAMM
LinkDB: A0A0C5VBX4_9GAMM
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ID   A0A0C5VBX4_9GAMM        Unreviewed;       402 AA.
AC   A0A0C5VBX4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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|ARBA:ARBA00031911, ECO:0000256|RuleBase:RU364075};
GN   ORFNames=YC6258_04808 {ECO:0000313|EMBL:AJQ96840.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ96840.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ96840.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ96840.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) 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         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:RU004504};
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|ARBA:ARBA00006490, ECO:0000256|RuleBase:RU364075}.
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DR   EMBL; CP007142; AJQ96840.1; -; Genomic_DNA.
DR   RefSeq; WP_044618751.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5VBX4; -.
DR   STRING; 1445510.YC6258_04808; -.
DR   KEGG; gsn:YC6258_04808; -.
DR   PATRIC; fig|1445510.3.peg.4772; -.
DR   HOGENOM; CLU_003433_0_0_6; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000032266; 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364075};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364075};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   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:UP000032266};
KW   Transferase {ECO:0000256|RuleBase:RU364075, ECO:0000313|EMBL:AJQ96840.1}.
FT   DOMAIN          4..366
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   402 AA;  43738 MW;  10EB05B9CDA553AC CRC64;
     MADIYLDNNA TTRVDPLVVE AMLPYFSEQF GNPSSLHSFG NKVGFAIKQA RKQIQQLIGA
     EHESEIIFTS CGTESDTTAI MSALAAQPER KEVITTVVEH PAILSLVDHL ESEGYTIHRL
     AVDNKGRLDL DEYRARLSDR VAIVSVMWAN NESGTLFPVE KMAEMAADAG VMFHTDAVQA
     AGKIAINVAE SDIHMLSISG HKLHAPKGIG VLYLKRGTRF RPYLRGGHQE RGRRAGTENT
     ASIIGLGKAA ELAMIHMETE NTEVRAMRDR LEQGLLSAIP YSFVTGDPDN RLPNTVSIAF
     EYIEGEAILL LLNKMGIAAS SGSACTSGSL EPSHVMRAMG IPYTAAHGTV RFSLSRYNTM
     AEVERVIEAV PPIVAKLRKL SPYWGANGPI AEQGQEFAPA YG
//
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