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Database: UniProt
Entry: A0A0H2KMZ0_9MICO
LinkDB: A0A0H2KMZ0_9MICO
Original site: A0A0H2KMZ0_9MICO 
ID   A0A0H2KMZ0_9MICO        Unreviewed;      1028 AA.
AC   A0A0H2KMZ0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KLN33229.1};
GN   ORFNames=FB00_18715 {ECO:0000313|EMBL:KLN33229.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN33229.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN33229.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN33229.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) 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:KLN33229.1}.
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DR   EMBL; JNBQ01000041; KLN33229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2KMZ0; -.
DR   STRING; 264251.FB00_18715; -.
DR   PATRIC; fig|264251.5.peg.3796; -.
DR   Proteomes; UP000035265; 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   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; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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:UP000035265}.
FT   DOMAIN          82..298
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          657..690
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  108734 MW;  83183860291FF600 CRC64;
     MSAEIDATPT PAPQHDGNGS RRSGSRATTS PEAERAAALR EAERAADVAR TALAEALRTV
     VRGGVDSSTR RRAEYSTDAS NYRVVPEAVV YPQDADDVVA ALDVLRELEV PVTARGAGTS
     VAGNSIGPGV VLDFTRHVNR VLDVDPEART ARIEPGVVMS ALQQQAAPHG LRFGPDPSTQ
     NRATLGGMIG NNACGPHAVA YGRTVDNVIE LDVVDGHGRR FTAGKGDPTF AAVPGLAELV
     RENLALIRTE FGRFGRQVSG YSLEHLLPEN GSDLAKALVG TEGTLVTILE ATVRLVPVPS
     KPTLVVLGYP DMPSAADDVP TFLNLSPLAV EGLDARLVDV VRRAKGDASV PPLPPGAGWL
     MVEVGGATPE EAMANAEAIV AASGSEATMI LPAGPEATKM WQIRADGAGL AGRTPAGEQA
     WPGWEDSAVP PEKLGDYLRD LDALMARYGV DGLPYGHFGD GCVHLRIDIP LEASGSVLRT
     FMLEAAELVA KYGGSLSGEH GDGRARSELL PVMYSPEAIA LMEQFKALFD PRDVMNPGVV
     VRPSAVDDDL RRPHAHPLLS KVGASGTPGT STAAPAKVTK ISRRAGYQGF SFAHDHGDMT
     QAVHRCVGVG KCRADTSAAG GFMCPSYQAT KDEKDVTRAR ARVLQEAVNG TLVGGLAAPE
     VRDSLDLCLS CKACSSDCPA GVDMAQYKSE VLYRTYRGKL RPVDHYSLGW LPIWARLATG
     MPRLANKLLG FRPLAKTVLW AGGMDTRRSM TTFAEVPFRT WWKRGGATQG VPGLRIGERP
     GHPVRDERPK VVLWTDSFSD NMSPGVPQAA VKVLTAAGYD VVVPDEQACC GLTWISTGQL
     DGARKRLENL LSVLGPYAVN GIPIMGLEPS CTAVLRSDLV DLFPDDPRAQ AVSAATRTLA
     ELLTSVDTAP GRESGWRVPD LSDVTAVVQP HCHQHSVMGF AADERLLRDA GATIKVLAGC
     CGLAGNFGMQ KGHYETSVAV AENALLPALR DAAPGDVYLA DGFSCRTQAD DLAGVQGKAL
     VELLAERL
//
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