ID A4BVK7_9GAMM Unreviewed; 397 AA.
AC A4BVK7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Cysteine sulfinate desulfinase/cysteine desulfurase and related enzyme {ECO:0000313|EMBL:EAR20272.1};
GN ORFNames=NB231_12986 {ECO:0000313|EMBL:EAR20272.1};
OS Nitrococcus mobilis Nb-231.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Nitrococcus.
OX NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR20272.1, ECO:0000313|Proteomes:UP000003374};
RN [1] {ECO:0000313|EMBL:EAR20272.1, ECO:0000313|Proteomes:UP000003374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nb-231 {ECO:0000313|EMBL:EAR20272.1,
RC ECO:0000313|Proteomes:UP000003374};
RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR20272.1}.
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DR EMBL; AAOF01000027; EAR20272.1; -; Genomic_DNA.
DR RefSeq; WP_005003285.1; NZ_CH672427.1.
DR AlphaFoldDB; A4BVK7; -.
DR STRING; 314278.NB231_12986; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_1_6; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000003374; 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 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; 1.
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 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:UP000003374}.
FT DOMAIN 7..373
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 397 AA; 42068 MW; 2EC06EFACF037121 CRC64;
MKIKETVYLD HQATTSVDSH VLAEMIPYFS DSFGNPHSSD HYLGWVSSRA VEDAAARVAR
LIGADADEII FTSGATESNN LALLGLGRRA VGGKRDRVLL SAIEHKCVLS VGRVLQEQYG
FRVDLIPVDS EGFVDLSVLE EMLGEDVLAV SVMAVNNEIG TIQDIAQVSK LAWSRGAVVH
CDAAQAPVAM NLEGIAGQSD IVSLSAHKMY GPKGIGVVYI SRELQGKVEP LIYGGGQQDG
LRSGTLPVPL CVGMGAAADL LAGDDAEDWR AELHRRRDAF VEKLSGLTWP VELNGPVGHV
RHPGNANIRF VGFSAHDILS ALQPRLAAST GSACTSGIPE PSYVLRAIGL DSDEAESSIR
FSLGFGTSDE DVAEAVGLIE EILAKLSKAK AGALSLS
//
