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Database: UniProt
Entry: K6XM00_9ALTE
LinkDB: K6XM00_9ALTE
Original site: K6XM00_9ALTE 
ID   K6XM00_9ALTE            Unreviewed;       486 AA.
AC   K6XM00;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=GARC_4751 {ECO:0000313|EMBL:GAC21689.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC21689.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC21689.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC21689.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAC21689.1}.
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DR   EMBL; BAEO01000065; GAC21689.1; -; Genomic_DNA.
DR   RefSeq; WP_007624942.1; NZ_BAEO01000065.1.
DR   AlphaFoldDB; K6XM00; -.
DR   STRING; 493475.GARC_4751; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9800184at2; -.
DR   Proteomes; UP000006327; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2520; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR007173; ALO_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR010031; FAD_lactone_oxidase-like.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   NCBIfam; TIGR01679; bact_FAD_ox; 1.
DR   PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PIRSF; PIRSF000136; LGO_GLO; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006327}.
FT   DOMAIN          70..237
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   486 AA;  54006 MW;  AED106F311B326B1 CRC64;
     MKFNSVKINR RTVIKSIGAS LGVAATASLY GCSDSSSVKP AVVTAEKKPL GIIGKDGRRV
     LPWSNWSGNL KAQPSIRAVP KNEQQLVDLI KNSKQTIRCV GAGHSWTPLV PTEDTLISLA
     RFRGVKKVDS STMEAEIGAG TLLSQIGEPL WQQGVSLRNM PDIDTQALAG AIATSTHGTG
     IGYGSLSSDV SKMTIVDAKG EVHNCSATQN SELYNAARNN LGCLGVVTSA TLKVEKAYKL
     EEKSWVMPLE EALENAPELV TKNRNLEFFA FPYADYAVGL SLNEVPITTP DVEEVQQLEG
     ENPLMTLRSL GDYTESFSWL RSFMLNRAIS GIEPATRVNK SYRIFGNIRD IRFTEMEYSI
     PAESGPKCLK EILDTIKKHN IDVIFPIEYR YVKGDDVWLS PFYKRDTCSI SCHNFHDRDY
     KKYFAAVEPI FLKYDGRPHW GKVHTLTAAE FSTKYSMLNE FLKVRKEYDP EGLFLNAHIK
     QILGVS
//
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