ID A0A2T8HGS1_9SPHI Unreviewed; 347 AA.
AC A0A2T8HGS1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:PVH24648.1};
GN ORFNames=DC487_14070 {ECO:0000313|EMBL:PVH24648.1};
OS Sphingobacterium corticibacter.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=2171749 {ECO:0000313|EMBL:PVH24648.1, ECO:0000313|Proteomes:UP000245627};
RN [1] {ECO:0000313|EMBL:PVH24648.1, ECO:0000313|Proteomes:UP000245627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2c-3 {ECO:0000313|EMBL:PVH24648.1,
RC ECO:0000313|Proteomes:UP000245627};
RA Li Y.;
RT "Sphingobacterium cortibacter sp. nov.";
RL Submitted (APR-2018) 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:PVH24648.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QDKG01000005; PVH24648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T8HGS1; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000245627; 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; cd06214; PA_degradation_oxidoreductase_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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
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:UP000245627}.
FT DOMAIN 1..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 259..347
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 347 AA; 39590 MW; BDE86F9E814591EA CRC64;
MHKFQISQII RQPNDNITIT FEDINKDFPP YLAGQFLTLV FDFNGRQVRR SYSFSSSPVV
DEPMAITVKR VDNGEISRLL HHRTSVGDTI EVMAAQGLLA YKPQADVPKT LFLFAAGVGV
TPLFSILKTA LVAEPDTKVV LVYSNGSSER TLFWNELREW QAKYPDRLHI EWIFSNSKNL
LTARLNREYI IRLVQQFDDP LKKTAIYLCG PVFYMDLCRF TLLGMGFPDE DIHKETFFFP
EEEADDDEHE EEEADTNTYQ VVLKFQGQSY DLAIPYNKTI LDVGLEQKIK LPYSCKSGMC
STCISQVHAG SVRMTYNEVL TDREVDNGRC LICTSHPVED GVVVEVL
//
