ID E5B4Z2_ERWAM Unreviewed; 1039 AA.
AC E5B4Z2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Uncharacterized protein ydiJ {ECO:0000313|EMBL:CBX80545.1};
GN Name=ydiJ {ECO:0000313|EMBL:CBX80545.1};
GN ORFNames=EAIL5_1725 {ECO:0000313|EMBL:CBX80545.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX80545.1};
RN [1] {ECO:0000313|EMBL:CBX80545.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX80545.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FR719190; CBX80545.1; -; Genomic_DNA.
DR AlphaFoldDB; E5B4Z2; -.
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}.
FT DOMAIN 70..303
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1039 AA; 115476 MW; 1E95763D17CE7544 CRC64;
MIKRTTAHFS NAIDSHNFGL AIMIPQISQA PGLAPQVLNF LAALKQQGFS GDMTTRYADR
LTMSTDNSIY QLLPDAVIFP RSTNDVAIIA SLAADGRFAS LAFTPRGGGT GTNGQALNQG
IVVDMSRYMT GILDINVAEG WVKVEAGVVK DQLNAWLKPY GYFFSPELST SNRATLGGMI
NTDASGQGSL VYGKTSDHVL GLKAVLLGGD ILDTCAIPIG QAEEKAQKAG REGEIYRVVL
ERCRQQRQLI INKFPSLNRF LTGYDLRHVL SDDLEVVDLT RILCGAEGTL AFITEAKLDI
TPLPAVRRLI NIKYDSFDSA LRNAPLMVEA KALSVETVDS KVLNLAREDI VWHSVSELIT
DVADKEMLGL NMVEFAGNDR ALIDSQVESL CQRLDMLIAR QEGGVIGYQL CDDVSGIERI
YGMRKKAVGL LGNAKGSAKP IPFVEDTCVP PHHLADYIAD FRALLDGHNL SYGMFGHVDA
GVLHVRPALD MCDPQQEQLM KQISDEVVEL TARYGGLLWG EHGKGFRAEY SPSFFGEELY
NELRRIKTAF DPHNRLNPGK ICTPLGVDDP MLTVDATKRG SYDRQIPINV RGAWRGAMEC
NGNGLCFNFD VKSPMCPSMK ITRNRMHSPK GRATLTREWL RLLAEQGVDP LLLEKQLPVK
GVSLRGMIMR TRHSWQAKRG EYDFSHEVKE AMSGCLACKA CSTQCPIKID VPDFRSRFLQ
LYHTRYLRPA GDYLVATVES YAPMMARAPR TFNFFLRQPW VKTLSQRHIG MVDLPQLSSP
SLKQQLAGHR ALTTTLEMLE QMNSAQRASC VLVVQDPFTS YYEAQLVNDF VQLIDKLGYT
AVLLPFSPNG KAQHIKGFLQ KFARTAQKTA DFLNRVAQLK MPLVGVDPAL VLCYRDEYNQ
VLGDKRGDFH VQLVQEWLQS ALAEQQSRPQ RGEPWYLFGH CTEATALPGA VKQWETIFAR
FGARLENVNV GCCGMAGTYG HETKNLENSL GIYQLSWQQA LQKLPLQRCL ATGYSCRSQV
KRVEGSPLRH PLQALLQLI
//
