ID Q87IC2_VIBPA Unreviewed; 433 AA.
AC Q87IC2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Putative arylsulfatase regulator {ECO:0000313|EMBL:BAC62027.1};
GN OrderedLocusNames=VPA0684 {ECO:0000313|EMBL:BAC62027.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC62027.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC62027.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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DR EMBL; BA000032; BAC62027.1; -; Genomic_DNA.
DR RefSeq; NP_800194.1; NC_004605.1.
DR RefSeq; WP_011106325.1; NC_004605.1.
DR AlphaFoldDB; Q87IC2; -.
DR GeneID; 1191373; -.
DR KEGG; vpa:VPA0684; -.
DR PATRIC; fig|223926.6.peg.3620; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_10_0_6; -.
DR Proteomes; UP000002493; Chromosome 2.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21120; SPASM_anSME; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034491; Anaerob_Ser_sulfatase-maturase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR047207; SPASM_anSME.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR03942; sulfatase_rSAM; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF3; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDF00285; anaerobic_Ser-type_sulfatase-m; 1.
DR SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 27..252
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 433 AA; 49230 MW; 1102DADB19366EFD CRC64;
MSKISPRHST TMPIVPLKTA SKAPVSGAYD RRFHVMAKPG GAKCNIDCQY CFYLHKENLL
HQEKQPKMDD ATLEAFVKSY IESQDGEEIV FSWQGGEPTL LGLDYFRNVV ALQKKHQPKG
VRIENDLQTN GILLNDEWCA FLKEHNFLVG LSIDGPRELH DKYRKTRSGK PTFDLVMKAV
DKLQAHGVKF NALVTVNRHN AKYPLEVYRF LTQELGVTYI QFAPVVEAND FQTTAPQFWN
EQMIPTKGSD LAKPGHLMSV VTDWSVDPED WGRFLMATFE EWVNNDLGRV LVNLFETAVA
QVMGKPSQLC VTAEFCGKGL AIEHNGDVFS CDHYVYPEYK LANIHEHSLN DMAFSTRQYT
FGMAKRESLP TYCKQCPYLP YCWGECPKNR LIKTPNGEAG LNYLCSGIKM FFDYALPMLV
GLAQLLQSEE PQR
//
