ID   A9DHU0_9GAMM            Unreviewed;      1077 AA.
AC   A9DHU0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Aldehyde oxidoreductase {ECO:0000313|EMBL:EDP99139.1};
GN   ORFNames=KT99_17495 {ECO:0000313|EMBL:EDP99139.1};
OS   Shewanella benthica KT99.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=314608 {ECO:0000313|EMBL:EDP99139.1, ECO:0000313|Proteomes:UP000005839};
RN   [1] {ECO:0000313|EMBL:EDP99139.1, ECO:0000313|Proteomes:UP000005839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT99 {ECO:0000313|EMBL:EDP99139.1,
RC   ECO:0000313|Proteomes:UP000005839};
RA   Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:EDP99139.1}.
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DR   EMBL; ABIC01000050; EDP99139.1; -; Genomic_DNA.
DR   RefSeq; WP_005502467.1; NZ_ABIC01000050.1.
DR   AlphaFoldDB; A9DHU0; -.
DR   STRING; 314608.KT99_17495; -.
DR   Proteomes; UP000005839; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          784..957
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1077 AA;  116956 MW;  D5D4698D00D4B87D CRC64;
     MSSFNHLGKR INRVDGLGKV TGKAIYGDDI LIPGMLYGVC RYADIPAGKV LSIDTQVAEQ
     VLGVVKIARF NDVPGNPYAG VIIRDYPPII DNLVRFEGDV LAVIVAETYE AACLAADKIQ
     IEYDVFKPIC SVEDALKPGA RLIQPGSDSN IVASHHTEKG DVDLAFAACA QQIERTFNIG
     FQEHGYIEPE SITAYIDPSS SNLVLSGSIQ NPHRVRGFVA SYLALPESDV DVRRSVLGGS
     FGGKDDTIDH LSCRAALMAQ LTGRPVKFTY TREQSICESS KRHPYNMTYK VGFDDSGRIQ
     AMKIDILVES GAYAACTPFV TWRSVVQAAG PYDIENVRVD IKGVYTNNTY TAAMRGFGSP
     QVVYANESLM DEIAEICHIS AIKVRKINVL KQDSLSITGQ KFDKHKVSAV EVLERAVEES
     DYQAKLEKYS RLNAGTDHVK YGIGLALSYR GCSMGAEGVD TSSALVVLNS DASVNISTGV
     CENGQGLQTT MTIIAAEVFG IAIGEVKFTE PPTSLISDGG PTVASRATVT GGAAVKDGAE
     TLKARIFEVV ASELKVETLD QTLWRDGIIS NRDLPELQIS FKEAVNKAKW AGINLAAYGW
     FAQPEISWDE EKGTGSPYFT WVYGCQIAEV KVDTSTGKLE LLHVTAVHDV GQVINKTGFE
     GQVAGGIAQG FGLGVLEDYN IEFGELKTKN LDSYLLPTIK DIPAIKIIAI ENGDEACPFG
     AKSIGEPASE LAAAAINNAA CFALKKRIRQ LPLTLEQLVL GYNLKKPARQ SELLQDDGHK
     KHTHRLTDMH LVNPSDLTET LQLLSEGGYR PFAGGTDLLV QGRLHYSDDK FVNILGIDGL
     NEIVETESEV RIGSAVCFNR ILAHSSVIGH FPLLSQACQT IGSNQIRNRA TIGGNIINAA
     PCADSVPPLL VYEAEVELQS ATSSRRIPLS QFITGSYRTD IKVGELLTQV CIPKQNLGNV
     SHKYSQLGRR NALNISRLSI SCLMGFDSEG KVDLCRVVDG SLFSHSQRLS AIEDLLIGSR
     LTSEVIGKAE NQLLDMIDTA IGGRWSAKYK QPVFINMFKD LMNDIVVENS QEQRDAC
//