dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; ;

CAZyme ID

MGYG000004061_00469

CAZy Family

GH19

CAZyme Description

Copper-exporting P-type ATPase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
905		94175.35	4.7197

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004061	1602330	MAG	United Kingdom	Europe

Gene Location

Start: 1315; End: 4032 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000004061_00469.

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
COG2217	ZntA	1	775	2	708	Cation transport ATPase [Inorganic ion transport and metabolism].
cd02094	P-type_ATPase_Cu-like	106	776	1	647	P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B. The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.
cd07552	P-type_ATPase_Cu-like	111	775	1	632	P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase. Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.
TIGR01525	ATPase-IB_hvy	177	774	1	558	heavy metal translocating P-type ATPase. This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512.
cd02079	P-type_ATPase_HM	121	773	4	617	P-type heavy metal-transporting ATPase. Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBQ55156.1	7.88e-108	167	778	123	704
AKG15649.2	2.76e-58	4	775	109	855
QWU86368.1	3.31e-22	224	721	2643	3182
QBQ55251.1	6.57e-22	221	721	96	697
QBQ55243.1	2.58e-21	219	782	81	747

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3J09_A	1.44e-167	1	779	2	716	Highresolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA [Archaeoglobus fulgidus],3J09_B High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA [Archaeoglobus fulgidus]
3RFU_A	3.30e-159	100	775	77	732	Crystalstructure of a copper-transporting PIB-type ATPase [Legionella pneumophila subsp. pneumophila str. Philadelphia 1],3RFU_B Crystal structure of a copper-transporting PIB-type ATPase [Legionella pneumophila subsp. pneumophila str. Philadelphia 1],3RFU_C Crystal structure of a copper-transporting PIB-type ATPase [Legionella pneumophila subsp. pneumophila str. Philadelphia 1],3RFU_D Crystal structure of a copper-transporting PIB-type ATPase [Legionella pneumophila subsp. pneumophila str. Philadelphia 1],4BEV_A ATPase crystal structure with bound phosphate analogue [Legionella pneumophila],4BYG_A ATPase crystal structure [Legionella pneumophila subsp. pneumophila str. Philadelphia 1]
4BBJ_A	3.62e-158	100	775	77	732	Copper-transportingPIB-ATPase in complex with beryllium fluoride representing the E2P state [Legionella pneumophila subsp. pneumophila]
3J08_A	1.00e-153	149	779	38	638	Highresolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA [Archaeoglobus fulgidus],3J08_B High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA [Archaeoglobus fulgidus]
7SI3_A	4.31e-120	7	784	567	1389	ChainA, P-type Cu(+) transporter [Xenopus tropicalis],7SI6_A Chain A, P-type Cu(+) transporter [Xenopus tropicalis],7SI7_A Chain A, P-type Cu(+) transporter [Xenopus tropicalis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37279	4.97e-182	2	779	4	746	Probable copper-transporting ATPase PacS OS=Synechococcus elongatus (strain PCC 7942 / FACHB-805) OX=1140 GN=pacS PE=3 SV=2
P58341	1.24e-179	3	780	84	826	Copper-transporting ATPase 1 OS=Rhizobium meliloti (strain 1021) OX=266834 GN=actP1 PE=3 SV=1
O32220	1.32e-178	2	778	74	802	Copper-exporting P-type ATPase OS=Bacillus subtilis (strain 168) OX=224308 GN=copA PE=1 SV=2
P58342	6.82e-176	3	780	84	827	Copper-transporting ATPase 2 OS=Rhizobium meliloti (strain 1021) OX=266834 GN=actP2 PE=3 SV=1
Q9X5X3	1.65e-173	3	780	84	827	Copper-transporting P-type ATPase OS=Sinorhizobium medicae (strain WSM419) OX=366394 GN=actP PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
108	127
142	159
180	202
217	236
370	392
402	424
725	747

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