ID A0A255GIY6_9ACTN Unreviewed; 316 AA.
AC A0A255GIY6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OYO14303.1};
GN ORFNames=CGZ94_06675 {ECO:0000313|EMBL:OYO14303.1};
OS Enemella evansiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016499 {ECO:0000313|EMBL:OYO14303.1, ECO:0000313|Proteomes:UP000215896};
RN [1] {ECO:0000313|EMBL:OYO14303.1, ECO:0000313|Proteomes:UP000215896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 030167 {ECO:0000313|EMBL:OYO14303.1,
RC ECO:0000313|Proteomes:UP000215896};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) 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:OYO14303.1}.
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DR EMBL; NMVO01000012; OYO14303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255GIY6; -.
DR OrthoDB; 3807506at2; -.
DR Proteomes; UP000215896; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000215896}.
FT DOMAIN 1..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 230..316
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 316 AA; 35086 MW; 94FA5AEBBF635ECD CRC64;
MKMIDVQVAE VIDETPAVKS IRFVRSDGQP LGTYQAGAHV DVVGPTAITR QYSLCSTPDD
PDSYTVAVKR EEKSRGGSVA LHDLQVGDRL QISEPRNLMQ VELSARHHVL MAAGIGITPM
LSMARWLHVH GHSFELHYFA RSHEEAAFLP LLQDRCPDQL HTHLGLQPEE HQEVLEQALT
ELPDGSHVYV CGPGVFMDRV REVAEQVVPA EHVHQESFTA EEQPDARENA AFTVEFEGET
YEVPPDRSIV EVLRENGADV ETSCQEGICG TCIMSVLEGT PEHRDNVLTR SEKEAGETMA
ICVSRAKTPK LVLDYF
//
