fixN

Cytochrome c oxidase subunit 1 homolog

551 amino acids

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B.

Belongs to the heme-copper respiratory oxidase family.

61.843 kDa

MSIVQTPAKRMTGGELGLILVFAALGFFSIVVAAKAYTPEYAFHAYLFAAASIATVFVIGNRYMDRPAELPPQTIDGKPNYNMAPVKVGTLLAVFWGIAGFLIGVIIALQMAYPLFNFDLPWISFGRLRPLHTSAVIFAFGGNVLIATSFYVVQRTSHARLAGYLAPWFVVLGYNFFIVIAGTGYLLGITQGKEYAEPEWYADLWLTIVWVTYFLVFLGTVLKRKEPHIYVANWFYLAFILTIAVLHLGNNAAIPVSVFSPKSYIVWSGVQDAMVQWWYGHNAVGFFLTAGFLALMYYFIPKRADKPVYSYRLSIVHFWALIFLYIWAGPHHLHYTALPDWAQTLGMTFSIMLWMPSWGGMINGLMTLSGAWDKLRTDPIIRMMVVAVAFYGMATFEGPMMSVKSVNSLSHYTEWGIGHVHSGALGWVAYISFGAIYCLIPWLWNKREMYSMKAIEWHFWVSTLGIVLYICAMWVAGILQGLMWRAYTALGFLEYSFIETVEAMHPLYVIRAIGGILFLAGSLIMAWNVFMTITRAETVSQPSGAALAPAE

fixN

Cytochrome c oxidase subunit 1 homolog, bacteroid

549 amino acids

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B.

Belongs to the heme-copper respiratory oxidase family.

61.273 kDa

MSQPSISKSMTIGESGLAVVFAATAFLCVIAAAKALDAPFAFHAALSAAASVAAVFCIVNRYFERPAALPPAEINGRPNYNMGPIKFSSFMAMFWGIAGFLVGLIIASQLAWPALNFDLPWISFGRLRPLHTSAVIFAFGGNVLIATSFYVVQKSCRVRLAGDLAPWFVVVGYNFFILVAGTGYLLGVTQSKEYAEPEWYADLWLTIVWVVYLLVFLATIIKRKEPHIFVANWFYLAFIVTIAVLHLGNNPALPVSAFGSKSYVAWGGIQDAMFQWWYGHNAVGFFLTAGFLAIMYYFIPKRAERPIYSYRLSIIHFWALIFLYIWAGPHHLHYTALPDWTQTLGMTFSIMLWMPSWGGMINGLMTLSGAWDKLRTDPVLRMLVVSVAFYGMSTFEGPMMSIKVVNSLSHYTDWTIGHVHSGALGWVGFVSFGALYCLVPWAWNRKGLYSLKLVNWHFWVATLGIVLYISAMWVSGILQGLMWRAYTSLGFLEYSFIETVEAMHPFYIIRAAGGGLFLIGALIMAYNLWMTVRVGEAEVQMPVALQPAE

fixN

Cytochrome c oxidase subunit 1 homolog

539 amino acids

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B.

Belongs to the heme-copper respiratory oxidase family.

60.651 kDa

MNYTLETADRALGAFPALLGAAFAHDSLFAAHMWVLFFTLVVSTLLLLRRVSFLPPVAGPPCRRTEYFDEVVKYGVMATVFWGVVGFLVGVVVALQLAFPDLNIAPYFNFGRMRPLHTSAVIFAFGGNALIATSFYVVQRTCRARLFGGNLGWFVFWGYNLFIIMAATGYLLGITQGREYAEPEWYVDLWLTIVWVAYLATFLGTILTRKEPHISVANWFYLSFIVTIAMLHIVNNLAVPVSFLGVKSYSAFSGVQAALTQWWYGHNAVGFFLTAGFLGMMYYFIPKQVNRPVYSYRLSIIHFWALIFMYIWAGPHHLHYTALPDWAQTLGMVFSIMLWMPSWGGMINGLMTLSGAWDKIRTDPIVRMMVMAVAFYGMATFEGPMMSIKAVNSLSHYTDWTIGHVHSGALGWNGMITFGAIYYLTPKLWGRDRLYSLQLVNWHFWLATLGIVVYAAVMWVAGIQQALMWREYDSQGFLVYSFAESVAALFPYYVMRALGGLMFLSGALIMAYNVTMTILGHQREEGASKGAAPSLQPAE

fixN

Cytochrome c oxidase subunit 1 homolog, bacteroid

539 amino acids

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B.

Belongs to the heme-copper respiratory oxidase family.

60.869 kDa

MKHTVEMVVLSVGAFLALVGAGLAQDRLFGAHMWVLFFALLAGTLVLMRRVDFRPAVAGHPGRRREYFDEVVKYGVVATVFWGVVGFLVGVVVALQLAFPELNVEPWFNFGRVRPLHTSAVIFAFGGNALIATSFYVVQRTSRARLFGGDLGWFVFWGYQLFIVLAASGYLLGITQSREYAEPEWYVDLWLTIVWVAYLVAFLGTIMKRKEPHIYVANWFYLAFIVTIAMLHVVNNLAVPVSFLGSKSYSAFSGVQDALTQWWYGHNAVGFFLTAGFLAMMYYFIPKQVNRPVYSYRLSIIHFWAIIFMYIWAGPHHLHYTALPDWAQTLGMVFSIMLWMPSWGGMINGLMTLSGAWDKIRTDPVVRMMVMAVAFYGMATFEGPMMSIKTVNSLSHYTDWTIGHVHSGALGWNGLITFGAIYYLVPKLWNRERLYSVRMVNWHFWLATLGIVVYAAVMWVAGIQQGLMWREYDDQGFLVYSFAETVAAMFPYYVMRAAGGALFLAGALLMAFNVTMTILGRVRDEEPIFGAAPLPAPAE