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Database: UniProt
Entry: G7HU75_9CORY
LinkDB: G7HU75_9CORY
Original site: G7HU75_9CORY 
ID   G7HU75_9CORY            Unreviewed;       962 AA.
AC   G7HU75;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=FAD linked oxidase domain-containing protein {ECO:0000313|EMBL:CCE53740.1};
GN   ORFNames=CCAS_00595 {ECO:0000313|EMBL:CCE53740.1};
OS   Corynebacterium casei UCMA 3821.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1110505 {ECO:0000313|EMBL:CCE53740.1, ECO:0000313|Proteomes:UP000004840};
RN   [1] {ECO:0000313|EMBL:CCE53740.1, ECO:0000313|Proteomes:UP000004840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCMA 3821 {ECO:0000313|EMBL:CCE53740.1,
RC   ECO:0000313|Proteomes:UP000004840};
RX   PubMed=22247534; DOI=10.1128/JB.06496-11;
RA   Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P.,
RA   Landaud S., Irlinger F.;
RT   "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a Smear-
RT   Ripened Cheese.";
RL   J. Bacteriol. 194:738-739(2012).
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:CCE53740.1}.
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DR   EMBL; CAFW01000009; CCE53740.1; -; Genomic_DNA.
DR   RefSeq; WP_006821327.1; NZ_CAFW01000009.1.
DR   AlphaFoldDB; G7HU75; -.
DR   Proteomes; UP000004840; 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   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}.
FT   DOMAIN          47..264
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          605..635
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   962 AA;  104186 MW;  DDAEB35FC1061D88 CRC64;
     MVNLPEAPLN TLKFDRIDPS VFKRIARTGM REDMTTRAAY SSDASIFRRI PKAVLEPKSV
     EDIRDGIAVA KARGWSIISR GGGTSVAGNA IGTGLIIDTS RYFNRILDID GDNRTATVEP
     GVVCDALRDA VAEHGLTYGP DPSTHSRCTI GGMVANNACG SHSVAYGTAA ENLVSVTIML
     ANGEEVTFGS NGVSDENIDK QMHQLVDAHA NLIDAELGRF PRQVSGYGLH YLLDKHGFDA
     AKAIAGTEGT VGVITKMTVK LVEVPKVKAL AVLAFETVYD AASAAARLRL PGVATIEGMG
     GDLLDALRSK RGQEKAGGNL PGNRKGIPAG GWLYCEVGGD TFEEAEALAE TVAAFVATVD
     SVVVSNPQEM RELWRIREAS AGVVTRLPDG GEAWPNWEDS AVPPENLADY LRDLYALMDK
     YSLRGIPFGH FGEGCVHVRI SFDFGSEEGI EIFNKFMNEA AELVSSYDGS LSGEHGDGRA
     RSALLDRMYS EEMRELFKQF KNILDPDGLF NPGVLVDPDE VTDGLRMAPG QRKFELTPVH
     KFSHDHGSMV NAVNRCVGVS ACRSEENSMC PSFQITGDEV HSTRGRARLL SEMFRGESVA
     DGYKSEEVLE ALDLCLSCKA CASECPVNVD MATYKSEFLH KHYKGKIRPM AHYMMGWLPL
     LGHIAHKVPL LPRIIDMSMR TPVLRTVIAK VGGLDTSRPL IRFAPSSLRK WHKKRSNNQA
     TKTVVLWPDS FNASLDTSPA TAAVEVLETL GYRVEIPQEF VCCGLTWHST GQLDMTQRVL
     KQTAKVMKPY TDRGLTVIGI EPSCTVMLKG EATELSDDPA IHQLAKSTVS FAEFVAPLIK
     EKVDSGEIQP ANISALTQVH CHEKSLGDPQ HSAKLLDALG VSQSDIETGC CGLAGNWGFE
     KGHAEMSMAL GERELFPKVR DAGAQGNAVI ADGFSCRTHI DQGTGVAPQH VAEIVRNVLK
     GD
//
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