ID A0A1R1IFQ6_9ACTN Unreviewed; 916 AA.
AC A0A1R1IFQ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:OMG57597.1};
GN ORFNames=BJN44_05785 {ECO:0000313|EMBL:OMG57597.1};
OS Tessaracoccus sp. ZS01.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1906324 {ECO:0000313|EMBL:OMG57597.1, ECO:0000313|Proteomes:UP000187142};
RN [1] {ECO:0000313|EMBL:OMG57597.1, ECO:0000313|Proteomes:UP000187142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS01 {ECO:0000313|EMBL:OMG57597.1,
RC ECO:0000313|Proteomes:UP000187142};
RA Salah Z., Rout S.P., Humphreys P.N.;
RT "Range of isolates obtained from hyperalkaline sediments.";
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};
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:OMG57597.1}.
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DR EMBL; MTHC01000003; OMG57597.1; -; Genomic_DNA.
DR RefSeq; WP_076060640.1; NZ_PQFE01000003.1.
DR AlphaFoldDB; A0A1R1IFQ6; -.
DR STRING; 1906324.BJN44_05785; -.
DR Proteomes; UP000187142; 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:UP000187142}.
FT DOMAIN 28..239
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 568..599
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 916 AA; 97016 MW; 5E39164B952E75B0 CRC64;
MSELGELASI VDTSTLTRAL YSSDASLYRV EPLAVAHPRT SDELIALVRA CLATDTPITA
RGAGTSCAGN AVGPGLVIDV AKHLHTIHSI DPVTGTAVID PGVVQDQLQI AARPYGLRLG
PDPSTSSRCT VGGMIGNNAC GPRALGYGRM SDNVVSLDII TGTGELLTLG VDDVPELRTL
VAANLGVIRT EFGTFIRQVS GYSPEHLLPE KKFDLPKFFA GTEGTLGVIV RATVRLVTDA
PVSVMVALGY PTMPDAGDDI ANLLRFQPTA CEGIDRRIVD VVIAKNGPEA VGELPAGDGW
MFLELVGDDR AEVLERAHAV VAGSAATEGW VVDDPARAIS LWKIRADGAG LAGVSLEKPA
YGGWEDAAVP PQHLGEYLRR FDELLGRYNL HGLPYGHFGD GCVHCRIDFP LTEPDGAERY
KAFVEEAAQL VASFGGSMSG EHGDGRARSA LLHHMYSPEA LGLFRQIKNV FDPKGLLNPG
VLVDPAPIEA DLRMVAASRS PLSLSDADFV EAVHQCSGVG KCLANSTAAG GVMCPSYQAT
RNEKDSTRGR ARALQEMVNG SLITGGWRSP EVHAALDLCL SCKGCARDCP TGVDMAAYKA
RVIHETYKGR LRPRAHYALG WLPRWGRLIT RVPGLGRLVN LVGGAPVLGR LLKFAAGVDG
RRQIPRFASK TARSSLSLGA VEGAKGRVLI WVDSFSDCFE STSFAAMVQV LVRLGYEPEV
LEETACCGLT WISTGQLDGA RRQLTNAAAV LARYVRDGVP IVGVEPSCTA VWRSDAPELL
PEDANVAALN GKVLTLAEFL TADPDFTPPD LSGHTIVAQP HCHHASVIGW AKDQAILLQT
GADLVQVGGC CGLAGNFGVE RGHHEVSVKV FEHDLGPAVE AHPDAIVLAD GFSCQTQLTS
LAGRSSMSLA ELLATH
//