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ASRA_SALTY
ID   ASRA_SALTY              Reviewed;         347 AA.
AC   P26474;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Anaerobic sulfite reductase subunit A;
DE   AltName: Full=Anaerobic sulfite reductase iron-sulfur subunit;
GN   Name=asrA; OrderedLocusNames=STM2548;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EB303;
RX   PubMed=1704886; DOI=10.1128/jb.173.4.1544-1553.1991;
RA   Huang C.J., Barrett E.L.;
RT   "Sequence analysis and expression of the Salmonella typhimurium asr operon
RT   encoding production of hydrogen sulfide from sulfite.";
RL   J. Bacteriol. 173:1544-1553(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Electron transfer protein for anaerobic sulfite reductase
CC       subunit A.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 2 [4Fe-4S] clusters.;
CC   -!- PATHWAY: Sulfur metabolism; sulfite reduction.
CC   -!- SUBUNIT: The anaerobic sulfite reductase seems to consist of three
CC       subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By sulfite. Repressed by oxygen.
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DR   EMBL; M57706; AAA99275.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21442.1; -; Genomic_DNA.
DR   PIR; A38453; A38453.
DR   RefSeq; NP_461483.1; NC_003197.2.
DR   RefSeq; WP_000985204.1; NC_003197.2.
DR   AlphaFoldDB; P26474; -.
DR   STRING; 99287.STM2548; -.
DR   PaxDb; P26474; -.
DR   EnsemblBacteria; AAL21442; AAL21442; STM2548.
DR   GeneID; 1254070; -.
DR   KEGG; stm:STM2548; -.
DR   PATRIC; fig|99287.12.peg.2688; -.
DR   HOGENOM; CLU_046702_0_1_6; -.
DR   OMA; THKLGTW; -.
DR   PhylomeDB; P26474; -.
DR   BioCyc; MetaCyc:MON-12544; -.
DR   BioCyc; SENT99287:STM2548-MON; -.
DR   UniPathway; UPA00370; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR014259; Sulphite_reductase_A.
DR   Pfam; PF17179; Fer4_22; 1.
DR   TIGRFAMs; TIGR02910; sulfite_red_A; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Cytoplasm; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..347
FT                   /note="Anaerobic sulfite reductase subunit A"
FT                   /id="PRO_0000159257"
FT   DOMAIN          219..251
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          302..331
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         230
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  39680 MW;  45B2C5DAEBF14296 CRC64;
     MAIKITPDEF SLLIQRLNKK WRVFAPSAEF RGGRFSDTDN IIYQRISGWR DLIWHEKSHM
     SPNTIIAPIT ETLFYFDKDT IQIAETDTSP IIIFARACDI NAMSRLDYMY LSNGNNSDYS
     YQLLREHIRF VLIECEESFE NCFCVSMGTN KTDCYSAAMR FSDEGALVSI RDPFIEAAIQ
     GLGQEADYTP SFVSENRETV VTPDSVCHDP QKIRDILTHH PLWDAYDSRC ISCGRCTTGC
     PTCTCYSVFD VAYDENPQRG ERRRQWASCM VPGFSDMAGG HGFREKPGER LRYRALHKVN
     DYKARNGIEH MCVGCGRCDD RCPQYIKFSL IINKMTAAVR QALAEEA
 
 
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