ID A0A0K2YCV4_9NOCA Unreviewed; 929 AA.
AC A0A0K2YCV4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CRK50781.1};
GN ORFNames=RHCRD62_20220 {ECO:0000313|EMBL:CRK50781.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK50781.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK50781.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK50781.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQP01000005; CRK50781.1; -; Genomic_DNA.
DR RefSeq; WP_050064083.1; NZ_CVQP01000005.1.
DR AlphaFoldDB; A0A0K2YCV4; -.
DR STRING; 260936.RHCRD62_20220; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000044872; 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; 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; 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:UP000044872}.
FT DOMAIN 33..246
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 929 AA; 98144 MW; 7603CC2ECCD935AF CRC64;
MSSAIATLRT RIAGEVDDAV RRRAEYSSDA SNYRVVPAAV VFPSSDDDVA AALAAGREYG
LPVTARGAGT SVAGNAIGPG LVLDFSRHLN RIVDLDGDAR TAVVQPGVVL STLQRAAAAH
GLRFGPDPST QDRCTIGGML GNNACGPRAV AWGRTADNTR TLRILDATDV ERTLADDLSA
VPGIDAFVTA NLATLRTELG RFDRQASGFS LEHLLPERGH ALAKAFVGTE GTCGLILDAT
VDLVPVPAAT ALAVLGYPDM PTAADDAVAL TVFEPLAVEG IDARLVDVVR RHKGPAAVPD
LPRGTGWLFV EMAGATTVDA IVAAEALCHS SSALDTRVLP TGPESAALWR IRADGVGLAG
RTRDGSPAWP GWEDAAVPQH RLGAYLRDFD DLMHGHDVDG LLYGHFGDGC VHIRLDFPFD
RAPHRFREFL VDAATLVAAH GGSMSGEHGD GRARSELLPL MYSPAALSTF AGFKALFDPD
GSLNPGVVVE PAAVDADLRV PAAAPAKGAG GFALLEDGGD LSVAAHRCVG IGKCRADSGA
SGGFMCPSYQ ATRDEKDSTR GRARVLQETI NGTLVTDGFA SEELAESLDL CLSCKACASD
CPAGVDMATY KSEVLHRRYR RRLRPLSHYT LGQMSRWTGI ASAAPRFTNA LARVGPLRRG
GMRLAGLDTR RDVPEVAAQS FRRWWRRRAP RTGGRDVLLW VDTFTDGFAP DAARDAVGLL
ESAGYRVTLT ERRVCCGLTW ISTGQLGGAR KQLTATLDQL EPHLDAGVPI IALEPSCAAV
LRSDLVELLP EDPRSPRVAS ATTTLAEFLT MATTANGEPW QPPDLTGVEV VVQPHCHQHA
VMGFRPDRAL LDRAGATVHQ LAGCCGLAGN FGMERGHYDV SVAVAEAALL PALAAHPDAI
LLADGFSCRT QAAQLTGRTG VHLATLLRR
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