ID Q5V6A7_HALMA Unreviewed; 721 AA.
AC Q5V6A7;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Possible hypoxanthine oxidase XdhD {ECO:0000313|EMBL:AAV44945.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:AAV44945.1};
GN Name=xdhD1 {ECO:0000313|EMBL:AAV44945.1};
GN OrderedLocusNames=pNG7244 {ECO:0000313|EMBL:AAV44945.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OG Plasmid pNG700 {ECO:0000313|EMBL:AAV44945.1,
OG ECO:0000313|Proteomes:UP000001169}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV44945.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV44945.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809
RC {ECO:0000313|Proteomes:UP000001169};
RC PLASMID=Plasmid pNG700 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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DR EMBL; AY596296; AAV44945.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5V6A7; -.
DR EnsemblBacteria; AAV44945; AAV44945; pNG7244.
DR KEGG; hma:pNG7244; -.
DR PATRIC; fig|272569.17.peg.674; -.
DR HOGENOM; CLU_001681_2_1_2; -.
DR Proteomes; UP000001169; Plasmid pNG700.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-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 SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AAV44945.1};
KW Plasmid {ECO:0000313|EMBL:AAV44945.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169}.
FT DOMAIN 2..75
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|Pfam:PF01315"
FT DOMAIN 115..351
FT /note="Aldehyde oxidase/xanthine dehydrogenase first
FT molybdopterin binding"
FT /evidence="ECO:0000259|Pfam:PF02738"
FT DOMAIN 386..654
FT /note="Aldehyde oxidase/xanthine dehydrogenase second
FT molybdopterin binding"
FT /evidence="ECO:0000259|Pfam:PF20256"
SQ SEQUENCE 721 AA; 78871 MW; AE0AE8E1F00C9CC0 CRC64;
MDGVDAVITP FDDVVPDKLY SSSGQSYPEP SPWDLKVLRE HVRFVGDPVA AVAADDPETA
DRAARKVEIE YRELDAVFDP EEALDEDAPQ LFEADDVENK QSGADYNRNL ESHFEGELGD
VNSAFERASN DDERHVIETE WETPYQSHCV PEPHTTIAYT DEDDRHVFIT ATQVPFHTRR
QIAHLFDVPI RDVRVKKPRI GAGFGSKQEM AIEPITFALH LAADRPVKLE MSRQEEFTAL
RFRHPMQMQM QTAVTDDGDI EAMDLYTLSN SGAYGTHGMT VANNVGTKPL PLYPRVSNVR
FSGDVVHTNL PMGAAMRGYG APQGHFAVEA HIDEVARRLD FDPIEFRLQN AVREGDLDRS
VAILKDGDRF TREIRSCGIR ECVDRGKEAI GYDDLEQPDE DHRKRGVGMA LIAQGSGVAG
KELGAAQVQM NEDGSFHLQV GGVDTGTGAD TMFSQIAAEV LGCTPEDVVV IAADTDLTPF
DYGAYASSTT YISGRAVKNA AEDAKERLLE WGAKLLEEPP DVLDTGDGGV YSERTGKRVS
LEEIGYEATY GDDEREHILG DGNHSTDESP PPYGAQFVDV TVDTETGEYE LNKLVFAADC
GVAINPALVE GQIEGGEHMS LEYATSGDLT FDEDGNPDVL GFRQYGMPRT TDHPEMETIL
VETHEPTGPF GAKSIAELPT NGVPPALSNA IRDAVGVRLT ELPFTAEDLM AALDDQSGAG
K
//
