Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Xanthine dehydrogenase molybdenum-binding subunit

Gene

xdhA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism) (By similarity).By similarity

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactori

Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Pathway: hypoxanthine degradation

This protein is involved in step 1 and 2 of the subpathway that synthesizes urate from hypoxanthine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Xanthine dehydrogenase iron-sulfur-binding subunit (xdhC), Xanthine dehydrogenase FAD-binding subunit (xdhB), Xanthine dehydrogenase molybdenum-binding subunit (xdhA)
  2. Xanthine dehydrogenase FAD-binding subunit (xdhB), Xanthine dehydrogenase molybdenum-binding subunit (xdhA)
This subpathway is part of the pathway hypoxanthine degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes urate from hypoxanthine, the pathway hypoxanthine degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi206 – 2061MolybdenumBy similarity
Metal bindingi237 – 2371Molybdenum; via carbonyl oxygenBy similarity
Metal bindingi350 – 3501Molybdenum; via amide nitrogenBy similarity
Metal bindingi516 – 5161Molybdenum; via amide nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism, Purine salvage

Keywords - Ligandi

Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3706-MONOMER.
ECOO157:Z4205-MONOMER.
UniPathwayiUPA00604; UER00661.
UPA00604; UER00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase molybdenum-binding subunit (EC:1.17.1.4)
Gene namesi
Name:xdhA
Ordered Locus Names:Z4205, ECs3739
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752Xanthine dehydrogenase molybdenum-binding subunitPRO_0000166089Add
BLAST

Interactioni

Subunit structurei

Heterotrimer of XdhA, XdhB and XdhC.Curated

Protein-protein interaction databases

STRINGi155864.Z4205.

Structurei

3D structure databases

ProteinModelPortaliQ8X6C7.
SMRiQ8X6C7. Positions 1-750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1529.
HOGENOMiHOG000244715.
KOiK00087.
OMAiAYVSHGH.
OrthoDBiEOG6ZSP3F.

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8X6C7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVDAIAKVT GRARYTDDYV MAGMCYAKYV RSPIAHGYAV SINDEQARSL
60 70 80 90 100
PGVLAIFTWE DVPDIPFATA GHAWTLDENK RDTADRALLT RHVRHHGDAV
110 120 130 140 150
AIVVARDELT AEKAAQLVSI EWEELPVITT PEAALAEDAA PIHNGGNLLK
160 170 180 190 200
QSTMSTGNVQ QTIDAADYQV QGHYQTPVIQ HCHMESVTSL AWMEDDSRIT
210 220 230 240 250
IVSSTQIPHI VRRVVGQALD IPWSCVRVIK TFVGGGFGNK QDVLEEPMAA
260 270 280 290 300
FLTSKLGGIP VKVSLSREEC FLATRTRHAF TIDGQMGVNR DGTLKGYSLD
310 320 330 340 350
VLSNTGAYVS HGHSIASAGG NKVAYLYPRC AYAYSSKTCY TNLPSAGAMR
360 370 380 390 400
GYGAPQVVFA VESMLDDAAT ALGIDPVEIR LRNASREGDA NPLTGKRIYS
410 420 430 440 450
AGLPECLEKG RKIFEWEKRR AECQNQQGNL RRGVGVACFS YTSNTWPVGV
460 470 480 490 500
EIAGARLLMN QDGTINVQSG ATEIGQGADT VFSQMVAETV GVPVSDVRVI
510 520 530 540 550
STQDTDVTPF DPGAFASRQS YVAAPALRSA ALLLKEKIIA HAAVMLHQSA
560 570 580 590 600
MNLTLIKGHI VLVERPEEPL MSLKDLAMDA FYHPERGGQL SAESSIKTTT
610 620 630 640 650
NPPAFGCTFV DLTVDIALCK VTINRILNVH DSGHILNPLL AEGQVHGGMG
660 670 680 690 700
MGIGWALFEE MIIDAKSGVV RNPNLLDYKM PTMPDLPQLE SAFVEINEPQ
710 720 730 740 750
SAYGHKSLGE PPIIPVAAAI RNAVKMATGV AINTLPLTPK RLYEEFHLAG

LI
Length:752
Mass (Da):81,370
Last modified:March 1, 2002 - v1
Checksum:iC42D8B8B7B386BB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57995.1.
BA000007 Genomic DNA. Translation: BAB37162.1.
PIRiC91096.
G85941.
RefSeqiNP_311766.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG57995; AAG57995; Z4205.
BAB37162; BAB37162; BAB37162.
GeneIDi916443.
KEGGiece:Z4205.
ecs:ECs3739.
PATRICi18356959. VBIEscCol44059_3658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57995.1.
BA000007 Genomic DNA. Translation: BAB37162.1.
PIRiC91096.
G85941.
RefSeqiNP_311766.1. NC_002695.1.

3D structure databases

ProteinModelPortaliQ8X6C7.
SMRiQ8X6C7. Positions 1-750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z4205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57995; AAG57995; Z4205.
BAB37162; BAB37162; BAB37162.
GeneIDi916443.
KEGGiece:Z4205.
ecs:ECs3739.
PATRICi18356959. VBIEscCol44059_3658.

Phylogenomic databases

eggNOGiCOG1529.
HOGENOMiHOG000244715.
KOiK00087.
OMAiAYVSHGH.
OrthoDBiEOG6ZSP3F.

Enzyme and pathway databases

UniPathwayiUPA00604; UER00661.
UPA00604; UER00662.
BioCyciECOL386585:GJFA-3706-MONOMER.
ECOO157:Z4205-MONOMER.

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiXDHA_ECO57
AccessioniPrimary (citable) accession number: Q8X6C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.