ID   A0A2A3AIT8_9MICC        Unreviewed;       963 AA.
AC   A0A2A3AIT8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:PBB09615.1};
GN   ORFNames=CKW39_00580 {ECO:0000313|EMBL:PBB09615.1};
OS   Kocuria sp. WRN011.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=2029858 {ECO:0000313|EMBL:PBB09615.1, ECO:0000313|Proteomes:UP000218573};
RN   [1] {ECO:0000313|EMBL:PBB09615.1, ECO:0000313|Proteomes:UP000218573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRN011 {ECO:0000313|EMBL:PBB09615.1,
RC   ECO:0000313|Proteomes:UP000218573};
RA   Zhang G., Wu G.;
RT   "Kocuria alkalisoli sp. nov., isolated from saline alkaline soil.";
RL   Submitted (AUG-2017) 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:PBB09615.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NSGI01000001; PBB09615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3AIT8; -.
DR   OrthoDB; 9770306at2; -.
DR   Proteomes; UP000218573; 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; 3.30.70.2740; -; 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:UP000218573}.
FT   DOMAIN          21..238
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          575..605
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   963 AA;  104120 MW;  434002F8E496BAD2 CRC64;
     MTALRDDLTT RAAYVSDASI YRRLPQAVAE PRSVDEIREL LATAQEKSWP VISRGGGTSV
     AGNAIGDGLI IDTSRYFNRI LEIDPDQGTA TIEPGVICDQ LRDAASEFGL TYGPDPSTHS
     RCTVGGMVAN NACGSHSVAW GTSASNLAAV TVMLADGREV TLEAGGTSDA ALDSQLKQLR
     DRHLAMLRTE LGQFPRQVSG YGLHYLLGEN GFDVAKAFSG TEGTCGIITQ LKVKLVAKPK
     FTALAVLGFK DAIEAATAAP KFRVPGVTTI EGMGSDLLTA LRTRQGQENA GGELPEGGGW
     LYCEVGADTQ EEAFEAARKL PALVKETVVD SVVVSDPTEA RALWRIREAG AGIVTRLPDG
     GEAWPGWEDS AVPPEHLGAY LKDLYELLDE MNLRGIPFGH FGEGCVHIRI SFDFNTDEGV
     ALYREFIERA AKLVHRYGGS VSGEHGDGRA RSELLTTIYS DEARQAFAEF KRIFDPENFF
     NPGVVVDPEP IDQGIRPGPG ARTFELTPVH AFSSDNGSFG QAINRCVGVG ACRSDSGAMC
     PSFVATGDEV HSTRGRMRSL AEMLRGEHIT DGWKSKETYE ALDLCLSCKA CATECPVNVD
     MATYKAEFLH HHFRQGLTSF IGKDRRPMAH LTMGWMPWLM KLVTKVPGSL RAVNFMERFR
     PVEELTKKLG GIEPQRRMIR FNNTPLTSWY KARTKGDDAA RDLARGGNRA SSAAGEKPSV
     VLWPDTFTNF SADAPGKAAI EVLEAMGYRV LMPMGNVCCG LTWHSTGQLD MTRKTLLQTL
     DVMEPLIEAG YPIIGLEPSC TVMLQHDITE LLPNDPRAHN VQALTVTLGE FSAKHAEEGG
     HWPFGTLETQ AGPGQALCQV HCHEQSMGDY SPELKVLEKL GVNSTVVGGG CCGLAGNWGF
     EPGHYEVSQT LGERELFPSI RAAEPGTIVL ADGFSCRTQV AQGTGAEGVH LAQVMRAAIR
     PEK
//