ID A0KPU0_AERHH Unreviewed; 464 AA.
AC A0KPU0;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:ABK39607.1};
GN OrderedLocusNames=AHA_3852 {ECO:0000313|EMBL:ABK39607.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39607.1, ECO:0000313|Proteomes:UP000000756};
RN [1] {ECO:0000313|EMBL:ABK39607.1, ECO:0000313|Proteomes:UP000000756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC KCTC 2358 / NCIMB 9240 / NCTC 8049
RC {ECO:0000313|Proteomes:UP000000756};
RX PubMed=16980456; DOI=10.1128/JB.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
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DR EMBL; CP000462; ABK39607.1; -; Genomic_DNA.
DR RefSeq; WP_011707552.1; NC_008570.1.
DR RefSeq; YP_858291.1; NC_008570.1.
DR AlphaFoldDB; A0KPU0; -.
DR STRING; 380703.AHA_3852; -.
DR EnsemblBacteria; ABK39607; ABK39607; AHA_3852.
DR KEGG; aha:AHA_3852; -.
DR PATRIC; fig|380703.7.peg.3823; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_3_6; -.
DR OrthoDB; 9800184at2; -.
DR Proteomes; UP000000756; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..198
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 51887 MW; EAA59E76EF453E0A CRC64;
MTVRFQAFHS IKAIGQREVL FNWSRTNPLG ALEQVWRPKN RDELQQLLRE NPERKLRLIG
SGLSFEPIHS VYAEGSQALL VDLHHLRGQL AKTVDTVTYQ AGTPLDTVYA DLIAMERMLP
ASPGVIGIQT LGGALSTGTH GQGLHQSALC DAVAAMTVML ASGDIIRVDR TDSRFGAFVM
GMGMLGILLD VTLQTVPNRI MRCTKFTTDY PFLLAHNERL NREHAFVKSW WFAWTGESHI
WLVDPASEEE VARYRAGGSE PLLLEGDIDA RMNATIDATL QKMAKDTKDE ALAGEHFETV
RRFKDASDLV GNVYQILCKG IPAPQINCEV AVPLHRMNEA LETLQAWQQA NPGVLHYPFI
LRCTGPSKAW LSAAYDQSVC WIGFLVYLAA DGTFVNGSME QMRELQQLLV PLGGIPHFGK
HLAMDLYDFP ALLPRWHDFL ALKGELDPHG RFENRWLADL FANR
//
