MULTISPECIES: NADPH-dependent assimilatory sulfite reductase

LOCUS       WP_000211913             599 aa            linear   BCT 20-NOV-2023
            flavoprotein subunit [Escherichia].
ACCESSION   WP_000211913
VERSION     WP_000211913.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008197.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10953
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..599
                     /gene="cysJ"
     Protein         1..599
                     /product="NADPH-dependent assimilatory sulfite reductase
                     flavoprotein subunit"
                     /EC_number="1.8.1.2"
                     /GO_function="GO:0004783 - sulfite reductase (NADPH)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0000103 - sulfate assimilation [Evidence
                     IEA]"
                     /GO_process="GO:0019344 - cysteine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66139
     Region          1..599
                     /region_name="cysJ"
                     /note="NADPH-dependent assimilatory sulfite reductase
                     flavoprotein subunit; PRK10953"
                     /db_xref="CDD:182862"
     Site            order(275,386..389,404,406,419..422)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99796"
     Site            order(386,388..389)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99796"
     Site            order(389,552,597,599)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99796"
     Site            order(406..409,460,462,489..490,519..520,527,529,558)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99796"
     Site            order(419,422,425)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99796"
     Site            order(457,461..464,466)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99796"
ORIGIN      
        1 mttqvppsal lplnpeqlar lqaattdltp tqlawvsgyf wgvlnqqpaa laatpapaae
       61 mpgitiisas qtgnarrvae alrddllaak lnvklvnagd ykfkqiasek llivvtstqg
      121 egeppeeava lhkflfskka pklentafav fslgdssyef fcqsgkdfds klaelggerl
      181 ldrvdadvey qaaasewrar vvdalksrap vaapsqsvat gavneihtsp yskdaplvas
      241 lsvnqkitgr nsekdvrhie idlgdsgmry qpgdalgvwy qndpalvkel vellwlkgde
      301 pvtvegktlp lnealqwhfe ltvntanive nyatltrset llplvgdkak lqhyaattpi
      361 vdmvrfspaq ldaealinll rpltprlysi assqaevene vhvtvgvvry dvegraragg
      421 assfladrve eegevrvfie hndnfrlpan petpvimigp gtgiapfraf mqqraadeap
      481 gknwlffgnp hftedflyqv ewqryvkdgv ltridlawsr dqkekvyvqd klreqgaelw
      541 rwindgahiy vcgdanrmak dveqallevi aefggmdtea adeflselrv erryqrdvy