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Database: UniProt
Entry: G7ZB91_AZOL4
LinkDB: G7ZB91_AZOL4
Original site: G7ZB91_AZOL4 
ID   G7ZB91_AZOL4            Unreviewed;       469 AA.
AC   G7ZB91;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Putative Fumarate reductase/succinate dehydrogenase flavoprotein {ECO:0000313|EMBL:CBS88530.1};
GN   OrderedLocusNames=AZOLI_p10238 {ECO:0000313|EMBL:CBS88530.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88530.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88530.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p1 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FQ311869; CBS88530.1; -; Genomic_DNA.
DR   RefSeq; WP_014187988.1; NC_016585.1.
DR   AlphaFoldDB; G7ZB91; -.
DR   KEGG; ali:AZOLI_p10238; -.
DR   HOGENOM; CLU_011398_4_3_5; -.
DR   OMA; HNEQMRV; -.
DR   OrthoDB; 3178130at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p1.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:CBS88530.1}.
FT   DOMAIN          18..434
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   469 AA;  48343 MW;  A05FFA4C7904E011 CRC64;
     MSRILPADGV EFEFTVPVVV IGGGAAGMVA ALAAHEQGAG VLVLERDALP QGSTALSAGL
     VPAPGTRWQR DAGIEDSPER FAADIIAKAK GEPDPAAVAR VAQAVGPALE WLADRYGLPF
     SVVDNFSYPG HSARRMHGLP SRSGAELIDR LRGAVETAGI DVLCEAHVTA LYADGALVRG
     VEITRPDGSV ERVGCGALIL ACNGYGGNRA LVERHVPELA DALYFGHPGN QGDALLWGEA
     LGAATRHLSG HQGHGSVAHP AGILVTWATI TEGGVQVNAQ GQRFSNEAQG YSEQAAIVLR
     QPDGIAWTVF DERIAAIARQ FEDFRQAEAM GAVLSADTPA ELARLMRIDA DALTATLADI
     DRLKATGGTD CFGRDFTGAA PLVPPYRAVR VTGALFHTQG GLVVDDEARV LDGNGARLPN
     LYAAGGAACG VSGSKASGYL SGNGLLTAVA LGRIAGSAAA SAAKEETNR
//
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