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Database: UniProt
Entry: D5SSG2_PLAL2
LinkDB: D5SSG2_PLAL2
Original site: D5SSG2_PLAL2 
ID   D5SSG2_PLAL2            Unreviewed;      1020 AA.
AC   D5SSG2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ADG66710.1};
GN   OrderedLocusNames=Plim_0866 {ECO:0000313|EMBL:ADG66710.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG66710.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG66710.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001744; ADG66710.1; -; Genomic_DNA.
DR   RefSeq; WP_013109141.1; NC_014148.1.
DR   AlphaFoldDB; D5SSG2; -.
DR   STRING; 521674.Plim_0866; -.
DR   KEGG; plm:Plim_0866; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_0; -.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000002220; Chromosome.
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; 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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
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; 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:UP000002220}.
FT   DOMAIN          37..267
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1020 AA;  112313 MW;  C5657859B2319F50 CRC64;
     MEIWATRIKE DLSGLFRGKL DVSRVASIVY SQDGGVTREA PCGVALPEDA EDLVVLVQYC
     HEHSIPMTVR GAGTSLFGQS LGPGLIIDVS ASMNRVLSLS ERTVRVEPGI TIDELNRRLR
     PYGREFGVYP LDSAVATVGG IVGVDGIGPH GLRHGAAHDH VASLQVMLAR GTQFTAGLEP
     LAMPDRKATE NEPHQVKRTI ICRLESILRN EAALIKASQP GVTLLRRGGY QLRGVLTEER
     LDLCRLLVGS EGTLGLYTGI TLHTTPLPAH RGVLLLLCPT LDSAIEVVHQ VRVMEPAACD
     LVDRRILTLA RELDDRFLMI IPPTIEAAVL IEVTAETESE CREQLTSLRR CTARIAEGHL
     TAYEANSPSD VEFLWSLSRK ILPQLEKPRG GVRTVRIFDD LVVPPEALAE FLAKAHKAFQ
     TADISAVMYS HAAMGVVHFR PLLTDRATWP VAALEQLQYA LYEAAWSLGG CIGSTQGLGS
     LRTSALREQY GSLCDIFKEV KNIFDPEGLL APGHVVPAAA RVGWGTAFPS ANQQAKAVEP
     IHFSGRELKS TFEQELPAQA PTGELVELCH SWPQGEAIES VNACNGCGNC RREDRNHRMC
     PFFHVTHQEV SSPRAKAVVF RDILSGRLSP ETLTRPEMLP ILNSCFNCQQ CSLECPSHVD
     IPRMAIELKG QAAAQQGVSR VDWLLSRPDV WGPWGSWLAP VLNPLLNWGT FRRVLELLTG
     VARERRLPLF SRKSFLQQTA QQAVDVPRSA SEPVAGQKKP LQPVVYFVDH FANYHDTELA
     MAFSRVLEHL GFELIVPKGQ LASGMALISA GELPAARELA LENLRVLAPH ARDGLRIICT
     EPTAALCLKK EYPRLTQHPD AELVAQQTVE AGAFLAELAA QGRLPIPTEP LAMTPMRAVY
     HTPCHLKSLG ERQPLLEICR LIPKLELHAV ERGCSGMAGT FGLSSKHFQT SMKIGHELME
     TMRSRDWDFG VTECSGCRLQ MTQRTATPTL HPIKLMAMAY GLMPELKVRF KHQTRKYTLE
//
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