GenomeNet

Database: RefSeq
Entry: WP_070069329
LinkDB: WP_070069329
Original site: WP_070069329 
LOCUS       WP_070069329             444 aa            linear   BCT 01-APR-2023
DEFINITION  FMN-binding glutamate synthase family protein [Acinetobacter
            qingfengensis].
ACCESSION   WP_070069329
VERSION     WP_070069329.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter qingfengensis
  ORGANISM  Acinetobacter qingfengensis
            Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales;
            Moraxellaceae; Acinetobacter.
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Acinetobacter qingfengensis"
                     /db_xref="taxon:1262585"
     Protein         1..444
                     /product="FMN-binding glutamate synthase family protein"
                     /EC_number="1.4.-.-"
                     /GO_function="GO:0015930 - glutamate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016638 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors [Evidence IEA]"
                     /GO_process="GO:0006537 - glutamate biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47274
     Region          16..420
                     /region_name="GltS_FMN"
                     /note="Glutamate synthase (GltS) FMN-binding domain. GltS
                     is a complex iron-sulfur flavoprotein that catalyzes the
                     reductive synthesis of L-glutamate from 2-oxoglutarate and
                     L-glutamine via intramolecular channelling of ammonia, a
                     reaction in the plant, yeast...; cd02808"
                     /db_xref="CDD:239202"
     Site            order(95..98,125,142,164,170,190,233,262..264,303,305,
                     326..327,335,357,362)
                     /site_type="active"
                     /db_xref="CDD:239202"
     Site            order(95..98,125,142,164,233,262..263,303,305,326..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239202"
     Site            order(170,190,263..264)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239202"
     Site            order(335,357,362)
                     /site_type="other"
                     /note="3Fe-4S cluster binding site [ion binding]"
                     /db_xref="CDD:239202"
ORIGIN      
        1 mtqstthidp vlresatfdr ltiqeiqraa atgiydirgg gtkrklphfd dllllgasms
       61 ryplegyrek cgtevvlgtr fakkpihlki pvtiagmsfg alsanakeal grgasvvgts
      121 tttgdggmtp eerghsstlv yqylpsrygm npddlrkada ievvlgqgak pggggmllgm
      181 kvtervagmr tlpvgvdqrs acrhpdwtgp ddlaikiael reitdwekpi yvkigasrpy
      241 ydvklaikag advivldgmq ggtaatqevf iehvgipils aipqaiqalq emgmhrkvql
      301 ivsggirtga dvakamalga davaigtaal ialgdnhprl ddelkkigsa agyyddwqng
      361 rdpagittqd pelsshldpi eggrhianyl rvmvleaqtm aracgkshlh nldpedlval
      421 tvesaamarv plagtnwvpg qlty
//
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