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Database: UniProt
Entry: A0A3N0C3J4_9MICC
LinkDB: A0A3N0C3J4_9MICC
Original site: A0A3N0C3J4_9MICC 
ID   A0A3N0C3J4_9MICC        Unreviewed;      1027 AA.
AC   A0A3N0C3J4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:RNL57244.1};
GN   ORFNames=D7003_07435 {ECO:0000313|EMBL:RNL57244.1};
OS   Arthrobacter oryzae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=409290 {ECO:0000313|EMBL:RNL57244.1, ECO:0000313|Proteomes:UP000273807};
RN   [1] {ECO:0000313|EMBL:RNL57244.1, ECO:0000313|Proteomes:UP000273807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TNB02 {ECO:0000313|EMBL:RNL57244.1,
RC   ECO:0000313|Proteomes:UP000273807};
RA   Cho Y.-J., Cho A., Kim O.-S.;
RT   "Genome sequencing of Arthrobacter oryzae TNB02.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RNL57244.1}.
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DR   EMBL; RBED01000079; RNL57244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N0C3J4; -.
DR   OrthoDB; 9770306at2; -.
DR   Proteomes; UP000273807; Unassembled WGS sequence.
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; 3.30.70.2190; -; 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; 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; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
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; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273807}.
FT   DOMAIN          56..288
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          646..677
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1027 AA;  108731 MW;  7B92625E5919F791 CRC64;
     MIDAVHSPPG PATETGQSGG RAAAQPAVLA RLASAGVAAD SSPRRLAEYS YDASNYRVAP
     LAVVFPRTVE DVVAAVAACR ETATPLIGRG GGTSMAGNAM GPGVVLDFSR HMNGIHSIDE
     AAGTVAVDPG VVLSVLSREV EKATGSRYTF APDPSSKNRA TVGGSLGNDA CGNHSVRYGR
     TSDHVAEIDV VTSDGARLTA AATGLRATDP EDKASAARAA ALTASLKGLA SSHLSEFRIE
     LERIQRQVSG YHLANLLPER GFNVARALAG SEGTCAIIVG ARMKLVPKPA SALLVCLGYA
     DVVDAARDIE TILEFSPAAV EGIDEAIVDT MRFRRGDGSV LGLPEGKAWL YVDLDGDNPD
     EVRAEADRLL DRLKENGRLM DGRTVPDLQE RASLWRVRED GAGLSARLST GGESWPGWED
     SAVAPSKLAD YLSDFRELLA SHDLKGVMYG HFGAGCMHIR ITYDLRTDAG RAVFRTFTRE
     AAELVVRHGG SLSGEHGDGR ARSELLPLMY SPRMLAAFAS YRRIWDPAGI LNPGSLTEAD
     AMDANLALEG IPQRQWRTSF DLRPLGAGGG SATETDSPET SGGSGTDPWV HALQSCIGVG
     RCRTDSGGVM CPSYRATKDE KDSTRGRSRV LQDMVRGART VEEGWKSEEV REALDLCLSC
     KACSTDCPTG VDMATYKSEF FSHYYEGRRR PLSHFSLGWL PLWLRITGRM APLVNAVMST
     PLAKAASALG GLTTQRALPR FAGANEWRRE VAAAGVGPVQ KYDGGSHPAA DAVVLFVDTF
     TRGFRPEVAG AAARVLAGTG APTECSADAC CGLTWISTGQ LDTATKLLGN AAAALDDGTD
     RPIVVVEPSC AAALRKDLPE LVHTEQARRV AARVRSFASH IEALTKSGWQ PAPAEPLPEQ
     VVLQTHCHEY SVFGAGIQRS ALSAVGVTDI VDATGCCGVA GNFGFEKEHF DVSMLVAEQS
     LAPALRQTEA DSVVLTDGFS CAMQVQQLDD SRPGRHLAQL LDPGAQAAAS PKRNRKPLPS
     TPEKDPS
//
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