ID   A0A1X4NHX7_9RHOB        Unreviewed;       327 AA.
AC   A0A1X4NHX7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
DE   Flags: Fragment;
GN   ORFNames=MGEO_16380 {ECO:0000313|EMBL:OSQ47331.1};
OS   Marivita geojedonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Marivita.
OX   NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ47331.1, ECO:0000313|Proteomes:UP000193926};
RN   [1] {ECO:0000313|EMBL:OSQ47331.1, ECO:0000313|Proteomes:UP000193926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ47331.1,
RC   ECO:0000313|Proteomes:UP000193926};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSQ47331.1}.
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DR   EMBL; JFKC01000020; OSQ47331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X4NHX7; -.
DR   STRING; 1123756.MGEO_16380; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000193926; Unassembled WGS sequence.
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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 2.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Aminotransferase {ECO:0000313|EMBL:OSQ47331.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193926};
KW   Transferase {ECO:0000313|EMBL:OSQ47331.1}.
FT   DOMAIN          7..59
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          103..311
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OSQ47331.1"
SQ   SEQUENCE   327 AA;  33773 MW;  A73427F642A50C6F CRC64;
     AMIAAMDVAG NPSSVHAEGR AAKGLVERAR AQVATAFGAD GADVVFVSGA TEAAALACAG
     RGLLGAEVEH DAVRAWIDPV LSVDALGRVS VTESARSVLQ LANSETGIVQ DLPQGLAVVD
     ATQAFGKLPV AFNWLGCEMA LISAHKLGGP KGVGALVMKR GTDLAAQIRG GGQEMGRRSG
     TENVIGIAGF GAAAEAAVRD LDAGIWDRVE KLRNILDSAI EARAKETIFV GKDVRRLPNT
     TCFATPGWKG ETQVMQMDLA GFAISAGSAC SSGKVKASAV LTAMGFDTVT ASSAIRVSLG
     PQTTEDDVMR FAETWLTKLE KHRARAA
//