ID   A0A1I1KZ34_9ACTN        Unreviewed;       981 AA.
AC   A0A1I1KZ34;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:SFC66059.1};
GN   ORFNames=SAMN04487968_10974 {ECO:0000313|EMBL:SFC66059.1};
OS   Nocardioides terrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=574651 {ECO:0000313|EMBL:SFC66059.1, ECO:0000313|Proteomes:UP000198832};
RN   [1] {ECO:0000313|EMBL:SFC66059.1, ECO:0000313|Proteomes:UP000198832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFC66059.1,
RC   ECO:0000313|Proteomes:UP000198832};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOLB01000009; SFC66059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1KZ34; -.
DR   STRING; 574651.SAMN04487968_10974; -.
DR   OrthoDB; 9770306at2; -.
DR   Proteomes; UP000198832; 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; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; 2.
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; 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:UP000198832}.
FT   DOMAIN          38..266
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   981 AA;  107583 MW;  8CE22E0FDD4B7C2C CRC64;
     MSVLEDPDVL ARLRARVDGE VLADAGTRAA YSTDASNFRQ VPLAVITPHT TDAAVDAIRA
     CRDLGLPVLS RGGGTSLAGQ GTNEAVLIDF SQHCHRLLSV DAENRRCVVE PGIVLDDLNR
     RLEPTGLRFG PEPATHPNCT LGGMIGNNSC GATAQRTGKV VDNVVSLDVL LYDGTRLTVG
     PTSDDEYDEI VAGADRRAGI YRDLRRLRDE HLALIRTRYP KIPRRVSGYN LDSLLPEHGF
     DLAGLLVGSE STLITVLGAE LKLVPRVKER TLVVLGFPDI TRAADAVPQI VDHEPIALEG
     VDRFLIHDEQ LRGMNKQGLE ELPEGTGFLM AQFGGDTQEE ADDRAHAMLD ALGKSEHDPQ
     VVFYDDPARE DELWQVREAG LGATAHVPHK RDTFEGWEDS AVAPERLGDY LRDLRRLYED
     FGYADETGPA LYGHFGQGCV HTRIPFDLYS SEGVAAYRRF LERAADLVVS YGGSLSGEHG
     DGQTRGELLP RMLGEDVVAL FEEVKRIFDP DDRMNPGKVV HPAPLDSHLR LGADWAPRQT
     EALHFAFPHD GGSFGEAANR CVGVGKCRQL KNQDGSVMCP SYQVTREERH STRGRSRLLF
     EMLDGHRDGP IKDGWRSEEV KDALDLCLAC KGCKSDCPAG VDMATYKAEF LAHHYRHRLR
     PRADYAMGWL PDLARFVEGA GLAGAVNAAT RIRWVRRAAT RAAGLEDRRV PRFASPTLQQ
     WWAARDHRPA GTRGSVVLWP DTFTNRFHPE VGRAAVAVLE DAGWTVTMPT EPLCCGLTWI
     STGQLTTAKR RLRRTVEALA PHVRAGGLVV GLEPSCTSVF RSDARELLPE NQDVHRVGDH
     TVTLAELLTE HTPEWEPPRL DTTSGVAQVH CHQHAVLGWD ADAELLHRAG AEVERLDSGC
     CGLAGNFGFT AGHGEVSRAL AEQVLLPRLR DEPADAVVLA DGFSCRTQID ELDTTGHHGL
     HLAQLLAQGL EKHDNHEGAP E
//