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Database: UniProt
Entry: A4C0U7_9FLAO
LinkDB: A4C0U7_9FLAO
Original site: A4C0U7_9FLAO 
ID   A4C0U7_9FLAO            Unreviewed;       970 AA.
AC   A4C0U7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=FAD linked oxidase-like protein {ECO:0000313|EMBL:EAR13040.1};
GN   ORFNames=PI23P_10440 {ECO:0000313|EMBL:EAR13040.1};
OS   Polaribacter irgensii 23-P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR13040.1, ECO:0000313|Proteomes:UP000003053};
RN   [1] {ECO:0000313|EMBL:EAR13040.1, ECO:0000313|Proteomes:UP000003053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23-P {ECO:0000313|EMBL:EAR13040.1,
RC   ECO:0000313|Proteomes:UP000003053};
RA   Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR13040.1}.
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DR   EMBL; AAOG01000002; EAR13040.1; -; Genomic_DNA.
DR   RefSeq; WP_004570708.1; NZ_CH724148.1.
DR   AlphaFoldDB; A4C0U7; -.
DR   STRING; 313594.PI23P_10440; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_10; -.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000003053; 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   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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; IPR009051; Helical_ferredxn.
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; PF13534; Fer4_17; 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:UP000003053}.
FT   DOMAIN          35..274
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          617..648
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   970 AA;  107786 MW;  1921F531061C8BF1 CRC64;
     MIQDTVLKQL NASLLGEVFF DNLHKTLYAT DASVYRKIPL AVAYPKNGKD IKVLIDFATK
     NKSTLIPRTA GTSLAGQCVG DGIVVDVSKY FTAILSFDET AKTIKLEPGI VRDSLNVYLK
     PFGLFFGPNT STSNRCMMGG MVGNNSSGST SIKYGVTRDK VLEIEAILSD GSEALFKEIS
     SQEFIAKTKE NTVEGNIYKA IFEELSLVEN QNEIKKEFPK EIIHRRNTGY AVDEFLTSDL
     FGGTEPSINV AKFLSGSEGT LAFSTSMTLQ LDNLPPSESI MVCAHFTSIH ESLLATVTAM
     KHNLYNCELM DKTILDCTKS NREQAKNRFF LQGDPEAILM LEISANTIEA AETLADALIA
     DLKQHNFGYH HPKVYGKDIS KVHSLRKAGL GLLGNMIGDK KAVACIEDTA VALADLPDYI
     KEFTKLMDKY QQNAVYYAHA GAGELHLRPI LNLKKKEDVV LFRKITTETA ELVKKYKGSF
     SGEHGDGIVR AEFIPLMIGE QNYQLLRRIK KAFDPNNVFN KGKITDAFAM DESLRYEVDR
     KEPIIETLQD FSDNEGILKL AEKCNGSGDC RKPVEAGGTM CPSYRATKNE KDTTRARANM
     LRDVLTNNTA SNKFDSKELK EVLDLCLSCK ACASECPSNV DIATMKVEFL YQYQETNGYS
     FRSSLFANNV KYNKLGSIAP ALTNAILSTP IAKAIMGVAQ KRKVPKLAVK TLKSWYKKQP
     QSENKKIVYL FCDEFTNFYD VEIGKDAFHL FEKLGYNLQI VHHEESGRSF ISKGFLKEAK
     AVCNLNVAIF KDIVTEETPL IGIEPSAILT FKDEYIRLAD DKKSAENIAK NVFTFEEFIA
     KEMANGNLQK SLFTKEAKIL KIHGHCHQKA LSGTHASFQV LNFPENYSVT IINSGCCGMA
     GSFGYEKEHY ALSMQVGEDT LFPKIRNTPK ETEIVAAGTS CRHQIFDGTE RIAKHPITIL
     KEALSLADAN
//
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