ID A0A127JQP2_9BURK Unreviewed; 799 AA.
AC A0A127JQP2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:AMO22354.1};
GN ORFNames=UC35_04885 {ECO:0000313|EMBL:AMO22354.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO22354.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO22354.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO22354.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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DR EMBL; CP010951; AMO22354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127JQP2; -.
DR PATRIC; fig|94132.3.peg.979; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000070433; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 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; IPR014309; Xanthine_DH_Mopterin-bd_su.
DR NCBIfam; TIGR02965; xanthine_xdhB; 1.
DR PANTHER; PTHR11908:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000070433}.
FT DOMAIN 61..168
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 85876 MW; 02F6AF57CC087C23 CRC64;
MKPRAKEQAE FTSATGGGPA GAADAGERNL APATVSPHAP ARPHPAMATS RPHESARAHV
TGTATYIDDI PEIKGTLHAA PILSTVAHGR LLSVDPSAAL ALPGVRAVLL ASDIPGDPVL
ATFVHDEPVF ARDEVQHVGQ VVGLVVADSV MQARRAARQV RLEIEALPAI LSAREAHAQR
SYVLPPVTVR RGEPESALAR SRHRMQGRLE VGGQEHFYLE GQVAYAIPQE QGEWRIHSST
QHPGEVQHWV AHALGLENNA VTVECRRMGG GFGGKETQAG HMAVWAALAA RKCGRPVKLR
LDRDDDFMIT GKRHPFEYDY EAGFDDSGLL TALKLTMLAN CGFSADLSGP VADRAIFHTD
NAYFLSDVEI VSCRCRTNTQ SHTAFRGFGG PQGMILIEAI LGDIARTLGL DPLDVRKRNL
YGIADRNVTH YGMKVEDNIL APLLARLEES SEYRKRRADI AAWNATSAVI RRGLAITPVK
FGISFTATFF NQAGALVHVY TDGSVQVNHG GTEMGQGLNT KIAQVVADEL GVPFERVRST
AADTGKVPNA SATAASSSTD LNGRAAQYAA RNVRDNLAAF VAGLDGCGAG AVRFQGGEVI
SPHATRSFDE VVKTAYANRI QLWSDGFYRT PKIHYDKTTL SGRPFYYFAY GAACTEVAID
TLTGEHRVLK VDILHDVGTS LNPAIDIGQI EGGFIQGMGW LTSEQLVWNE QGQLATHAPS
TYKIPTAGDV PAHFYVQLWP EPNREDNVGG SKAVGEPPLM LAISVWEAIR DAVSGARGDR
RPVAMRAPAT PENVLAALA
//
