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Database: UniProt
Entry: A0A0U3JW88_9BURK
LinkDB: A0A0U3JW88_9BURK
Original site: A0A0U3JW88_9BURK 
ID   A0A0U3JW88_9BURK        Unreviewed;      1333 AA.
AC   A0A0U3JW88;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Oxidoreductase protein {ECO:0000313|EMBL:ALU91021.1};
GN   ORFNames=Hrubri_3869 {ECO:0000313|EMBL:ALU91021.1};
OS   Herbaspirillum rubrisubalbicans M1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU91021.1, ECO:0000313|Proteomes:UP000069903};
RN   [1] {ECO:0000313|EMBL:ALU91021.1, ECO:0000313|Proteomes:UP000069903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1 {ECO:0000313|EMBL:ALU91021.1,
RC   ECO:0000313|Proteomes:UP000069903};
RA   Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA   Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA   Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT   "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP013737; ALU91021.1; -; Genomic_DNA.
DR   RefSeq; WP_058896710.1; NZ_CP013737.1.
DR   STRING; 1078773.Hrubri_3869; -.
DR   KEGG; hrb:Hrubri_3869; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000069903; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR021817; DUF3400.
DR   InterPro; IPR022153; DUF3683.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF11880; DUF3400; 1.
DR   Pfam; PF12447; DUF3683; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 2.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          191..428
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1333 AA;  148043 MW;  291AA8CE1BB1C4DE CRC64;
     MNAPAQIQAL LTDAPHGAAL PRLREIPYNY TSFSDREIVI RLLGESSWSL LDELRGKRQT
     GRSARMLYEV LGDIWVVRRN PYLQDDLLDN PKRRAALIEA LNHRINEVDK RRLATDSAEA
     GDADAQRRSA SVEALLKAAK KAIGDFAEEF RQTYDLRRRA TKVLGRYTAR DNIKFDGLSR
     VSHVTDATDW RVEYPFVVLT PDTEDEMAGL VKACIELGLT IIPRGGGTGY TGGAIPLTPL
     SAVINTEKLE QLGAVEMTML PGVDKPYATI YSGAGVVTKR VSDAAEKAGF VFAVDPTSAE
     ASCIGGNVAM NAGGKKAVLW GTALDNLASW RMVDPQGDWL EVTRLDHNLG KIHDVEVARF
     KLEWSHPGEK GQKTEVFKTE ILEISGKKFR KEGLGKDVTD KFLSGLPGVQ KEGCDGLITS
     ARWILHKMPK QTRTVCLEFF GQARDAIPSI VEIKDYLDAE TKKGGAILAG LEHLDERYLR
     AVGYATKSKR GVLPKMVLIG DIVGDDENAV AAAASEVIRM ANNRVGEGFV AVSPEARKKF
     WLDRSRTAAI AKHTNAFKIN EDVVIPLNRM GEYTDGIERI NIELSIKNKL QLLAELDSFF
     VKGNLPLGKS DDAEGDDIPA AEMLEDRVHQ AESLLEQTHA RWSYLLANLD KPLGEAKGEL
     AALGLEKMLP VFEQRLIDQP EAAVFHVVQD RTVRISWKQE VRAQLRQIFS GAAFKPILEE
     CQAIHKRVLR GRVFVALHMH AGDGNVHTNI PVNSDHYDML QDAHVAVARI MKLARSLNGV
     ISGEHGIGIT KLEFLTEDEI GEFREYKKRV DPEGRFNKGK LLNLPGMEAD LSNAYTPSFG
     LMGHESLIMQ QSDIGAIASS VKDCLRCGKC KPVCSTHVPR ANLLYSPRNK ILATSLLVEA
     FLYEEQTRRG VSIKHWEEFE DVADHCTVCH KCVTPCPVDI DFGDVSMNMR NLLRKMGKKS
     FNAGTNAAMF FLNATDPATI NATRKVMTQW GFKAQRLGND LMKKFAKKQT QKPPATVGKP
     PVKEQVIHFI NKKMPGNLPK KTARALLDIE DDKIVPIIRN PKTTTADTEA VFYFPGCGSE
     RLFSQVGLAT QAMLWNVGVQ TVLPPGYLCC GYPQRGTGDF EKGEKIITDN RVLFHRMANT
     LNYLDIKTVV VSCGTCYDQL QGYEFEKIFP GCRIIDIHEY LLEKGVKLEG VTGTRYMYHD
     PCHSPMKQQD PLKTVNSLIT TVDAQKIEKN DRCCGESGTF GVSRPDVSTQ VRFRKEEEMK
     KGSDKVRADG FAGDVKILTS CPSCFQGLSR YNDDAGTTAD YIVVEMARHL LGENWMPEYV
     ERANNGGIER ILV
//
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