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Proteins in SwissProt homologous to 1n62B

47 proteins with E() < 0.001

Homologs in PDB


Acc   E.C. E() % id alen 388
&C
763
*E
P19919
DCML_OLICO
Carbon monoxide dehydrogenase large chai1.2.99.20100.0804 &C*E
P19913
DCML_HYDPS
Carbon monoxide dehydrogenase large chai1.2.99.2068.4788 &C*E
D7REY3
CDHA_PSEU3
Caffeine dehydrogenase subunit alpha; Ca1.17.5.22.7e-9035.6775 --*E
Q46814
XDHD_ECOLI
Probable hypoxanthine oxidase XdhD2.2e-4826.9802 --*E
Q8XD64
XDHD_ECO57
Probable hypoxanthine oxidase XdhD4.1e-4826.9802 --*E
Q46799
XDHA_ECOLI
Xanthine dehydrogenase molybdenum-bindin1.17.1.47.6e-4825.8770 --*E
O33819
HCRA_THAAR
4-hydroxybenzoyl-CoA reductase subunit a1.3.7.92e-4727.6773 --*E
Q8X6C7
XDHA_ECO57
Xanthine dehydrogenase molybdenum-bindin1.17.1.46.9e-4725.7770 --*E
O32144
XDHD_BACSU
Probable xanthine dehydrogenase subunit 1.17.1.49.7e-3626.2757 --*E
Q46509
MOP_DESGI
Aldehyde oxidoreductase; Molybdenum iron1.2.99.74.5e-3526.7776 --*E
Q6AUV1
XDH_ORYSJ
Xanthine dehydrogenase1.17.1.46.1e-2925.4778 --*E
Q0QLF2
NDLMS_EUBBA
Nicotinate dehydrogenase large molybdopt1.17.1.51.5e-2829.5447 ----
Q54FB7
XDH_DICDI
Xanthine dehydrogenase; Short=XD1.17.1.42.7e-2725.1744 --*E
Q12553
XDH_EMENI
Xanthine dehydrogenase; Purine hydroxyla1.17.1.43.7e-2724.2802 --*E
P91711
XDH_DROSU
Xanthine dehydrogenase; Short=XD; Protei1.17.1.49.2e-2725.3764 --*E
P10351
XDH_DROME
Xanthine dehydrogenase; Short=XD; Protei1.17.1.41.7e-2624.8782 --*E
P22811
XDH_DROPS
Xanthine dehydrogenase; Short=XD; Protei1.17.1.46.1e-2624.7770 --*E
P80457
XDH_BOVIN
Xanthine dehydrogenase/oxidase; Includes1.17.1.4, 1.17.3.21.1e-2526.1771 --*E
Q9MYW6
XDH_FELCA
Xanthine dehydrogenase/oxidase; Includes1.17.1.4, 1.17.3.22.1e-2524.0767 --*E
P08793
XDH_CALVI
Xanthine dehydrogenase; Short=XD1.17.1.41.4e-2423.3801 --*E
P47989
XDH_HUMAN
Xanthine dehydrogenase/oxidase; Includes1.17.1.4, 1.17.3.22.3e-2425.2769 --*E
Q7G9P4
ALDO3_ARATH
Abscisic-aldehyde oxidase; Aldehyde oxid1.2.3.14, 1.2.3.75e-2423.6770 &A*E
Q06278
ADO_HUMAN
Aldehyde oxidase1.2.3.18e-2426.1766 --*E
Q5FB27
ADO_MACFA
Aldehyde oxidase1.2.3.19.4e-2425.8766 --*E
Q8GUQ8
XDH1_ARATH
Xanthine dehydrogenase 1; Short=AtXDH11.17.1.49.6e-2423.7744 --*E
P48034
ADO_BOVIN
Aldehyde oxidase1.2.3.11.3e-2324.6760 --*E
F4JLI5
XDH2_ARATH
Xanthine dehydrogenase 2; Short=AtXDH21.17.1.41.8e-2324.5763 --*S
P47990
XDH_CHICK
Xanthine dehydrogenase/oxidase; Includes1.17.1.4, 1.17.3.21.8e-2322.8763 --*E
Q7G191
ALDO4_ARATH
Benzaldehyde dehydrogenase (NAD(+)); Ald1.2.1.28, 1.2.3.72.8e-2324.9772 &T*E
P80456
ADO_RABIT
Aldehyde oxidase; Retinal oxidase1.2.3.13.9e-2324.2785 --*E
Q8X6J4
YAGR_ECO57
Putative xanthine dehydrogenase YagR mol1.17.1.44.3e-2323.9784 &A*E
P77489
YAGR_ECOLI
Putative xanthine dehydrogenase YagR mol1.17.1.45.9e-2324.1785 &A*E
Q00519
XDH_MOUSE
Xanthine dehydrogenase/oxidase; Includes1.17.1.4, 1.17.3.26.2e-2324.2772 --*E
O23888
ALDO2_MAIZE
Indole-3-acetaldehyde oxidase; Short=IAA1.2.3.78.6e-2324.3774 &S*E
O23887
ALDO1_MAIZE
Indole-3-acetaldehyde oxidase; Short=IAA1.2.3.71e-2223.4774 &G*E
P22985
XDH_RAT
Xanthine dehydrogenase/oxidase; Includes1.17.1.4, 1.17.3.21.9e-2223.9785 --*E
Q7XH05
ALDO1_ORYSJ
Probable aldehyde oxidase 1; Short=AO-11.2.3.14.2e-2223.4785 &A*E
Q7G193
ALDO1_ARATH
Indole-3-acetaldehyde oxidase; Short=IAA1.2.3.74.2e-2223.2781 &A*E
Q6Z351
ALDOL_ORYSJ
Putative aldehyde oxidase-like protein4.8e-2223.4792 &A*E
Q852M2
ALDO3_ORYSJ
Probable aldehyde oxidase 3; Short=AO-31.2.3.11.3e-2123.7792 &G*E
Q9Z0U5
ADO_RAT
Aldehyde oxidase1.2.3.11.4e-2124.3761 --*E
O54754
ADO_MOUSE
Aldehyde oxidase; Retinal oxidase1.2.3.13.7e-2123.4761 --*E
Q852M1
ALDO2_ORYSJ
Probable aldehyde oxidase 2; Short=AO-21.2.3.15.2e-2123.9792 &G*E
Q7G192
ALDO2_ARATH
Indole-3-acetaldehyde oxidase; Short=IAA1.2.3.75.3e-2022.8776 --*E
Q0QLF1
NDMMS_EUBBA
Nicotinate dehydrogenase medium molybdop1.17.1.57.8e-1828.0307 --*E
Q51698
IORB_BREDI
Isoquinoline 1-oxidoreductase subunit be1.3.99.162.5e-1025.5420 &R--
Q69R21
ALDO4_ORYSJ
Probable aldehyde oxidase 4; Short=AO-41.2.3.10.0001323.8256 ----

Proteins identified as mutant are highlighted in maroon. Conservative changes in active site residues, e.g. &K, are marked in green. Non-conservative changes to active site residues (&A) are highlighted in red. Library sequence residues identical to MACie active site residues are shown in grey.

Likewise, E.C. numbers identical to the MACiE protein are shown in grey; differences in black.


Homologs in SwissProt for MACiE ID:


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