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}.
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; 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
//