IED Industry Enzyme Database

Detail Information for IndEnz0016000075
IED ID IndEnz0016000075
Enzyme Type ID tyrosinase000075
Protein Name Hemocyanin 1
Keyhole limpet hemocyanin A
KLH-A
Gene Name KLH1
Organism Megathura crenulata (Giant keyhole limpet)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Mollusca Gastropoda Vetigastropoda Lepetellida Fissurelloidea Fissurellidae Megathura Megathura crenulata (Giant keyhole limpet)
Enzyme Sequence MLSVRLLIVVLALANAENLVRKSVEHLTQEETLDLQAALRELQMDSSSIGFQKIAAAHGAPASCVHKDTSIACCIHGMPTFPHWHRAYVVHMERALQTKRRTSGLPYWDWTEPITQLPSLAADPVYIDSQGGKAHTNYWYRGNIDFLDKKTNRAVDDRLFEKVKPGQHTHLMESVLDALEQDEFCKFEIQFELAHNAIHYLVGGKHDYSMANLEYTAYDPIFFLHHSNVDRIFAIWQRLQELRNKDPKAMDCAQELLHQKMEPFSWEDNDIPLTNEHSTPADLFDYCELHYDYDTLNLNGMTPEELKTYLDERSSRARAFASFRLKGFGGSANVFVYVCIPDDNDRNDDHCEKAGDFFVLGGPSEMKWQFYRPYLFDLSDTVHKMGMKLDGHYTVKAELFSVNGTALPDDLLPHPVVVHHPEKGFTDPPVKHHQSANLLVRKNINDLTREEVLNLREAFHKFQEDRSVDGYQATAEYHGLPARCPRPDAKDRYACCVHGMPIFPHWHRLFVTQVEDALVGRGATIGIPYWDWTEPMTHIPGLAGNKTYVDSHGASHTNPFHSSVIAFEENAPHTKRQIDQRLFKPATFGHHTDLFNQILYAFEQEDYCDFEVQFEITHNTIHAWTGGSEHFSMSSLHYTAFDPLFYFHHSNVDRLWAVWQALQMRRHKPYRAHCAISLEHMHLKPFAFSSPLNNNEKTHANAMPNKIYDYENVLHYTYEDLTFGGISLENIEKMIHENQQEDRIYAGFLLAGIRTSANVDIFIKTTDSVQHKAGTFAVLGGSKEMKWGFDRVFKFDITHVLKDLDLTADGDFEVTVDITEVDGTKLASSLIPHASVIREHARVKFDKVPRSRLIRKNVDRLSPEEMNELRKALALLKEDKSAGGFQQLGAFHGEPKWCPSPEASKKFACCVHGMSVFPHWHRLLTVQSENALRRHGYDGALPYWDWTSPLNHLPELADHEKYVDPEDGVEKHNPWFDGHIDTVDKTTTRSVQNKLFEQPEFGHYTSIAKQVLLALEQDNFCDFEIQYEIAHNYIHALVGGAQPYGMASLRYTAFDPLFYLHHSNTDRIWAIWQALQKYRGKPYNVANCAVTSMREPLQPFGLSANINTDHVTKEHSVPFNVFDYKTNFNYEYDTLEFNGLSISQLNKKLEAIKSQDRFFAGFLLSGFKKSSLVKFNICTDSSNCHPAGEFYLLGDENEMPWAYDRVFKYDITEKLHDLKLHAEDHFYIDYEVFDLKPASLGKDLFKQPSVIHEPRIGHHEGEVYQAEVTSANRIRKNIENLSLGELESLRAAFLEIENDGTYESIAKFHGSPGLCQLNGNPISCCVHGMPTFPHWHRLYVVVVENALLKKGSSVAVPYWDWTKRIEHLPHLISDATYYNSRQHHYETNPFHHGKITHENEITTRDPKDSLFHSDYFYEQVLYALEQDNFCDFEIQLEILHNALHSLLGGKGKYSMSNLDYAAFDPVFFLHHATTDRIWAIWQDLQRFRKRPYREANCAIQLMHTPLQPFDKSDNNDEATKTHATPHDGFEYQNSFGYAYDNLELNHYSIPQLDHMLQERKRHDRVFAGFLLHNIGTSADGHVFVCLPTGEHTKDCSHEAGMFSILGGQTEMSFVFDRLYKLDITKALKKNGVHLQGDFDLEIEITAVNGSHLDSHVIHSPTILFEAGTDSAHTDDGHTEPVMIRKDITQLDKRQQLSLVKALESMKADHSSDGFQAIASFHALPPLCPSPAASKRFACCVHGMATFPQWHRLYTVQFQDSLRKHGAVVGLPYWDWTLPRSELPELLTVSTIHDPETGRDIPNPFIGSKIEFEGENVHTKRDINRDRLFQGSTKTHHNWFIEQALLALEQTNYCDFEVQFEIMHNGVHTWVGGKEPYGIGHLHYASYDPLFYIHHSQTDRIWAIWQSLQRFRGLSGSEANCAVNLMKTPLKPFSFGAPYNLNDHTHDFSKPEDTFDYQKFGYIYDTLEFAGWSIRGIDHIVRNRQEHSRVFAGFLLEGFGTSATVDFQVCRTAGDCEDAGYFTVLGGEKEMPWAFDRLYKYDITETLDKMNLRHDEIFQIEVTITSYDGTVLDSGLIPTPSIIYDPAHHDISSHHLSLNKVRHDLSTLSERDIGSLKYALSSLQADTSADGFAAIASFHGLPAKCNDSHNNEVACCIHGMPTFPHWHRLYTLQFEQALRRHGSSVAVPYWDWTKPIHNIPHLFTDKEYYDVWRNKVMPNPFARGYVPSHDTYTVRDVQEGLFHLTSTGEHSALLNQALLALEQHDYCDFAVQFEVMHNTIHYLVGGPQVYSLSSLHYASYDPIFFIHHSFVDKVWAVWQALQEKRGLPSDRADCAVSLMTQNMRPFHYEINHNQFTKKHAVPNDVFKYELLGYRYDNLEIGGMNLHEIEKEIKDKQHHVRVFAGFLLHGIRTSADVQFQICKTSEDCHHGGQIFVLGGTKEMAWAYNRLFKYDITHALHDAHITPEDVFHPSEPFFIKVSVTAVNGTVLPASILHAPTIIYEPGLDHHEDHHSSSMAGHGVRKEINTLTTAEVDNLKDAMRAVMADHGPNGYQAIAAFHGNPPMCPMPDGKNYSCCTHGMATFPHWHRLYTKQMEDALTAHGARVGLPYWDGTTAFTALPTFVTDEEDNPFHHGHIDYLGVDTTRSPRDKLFNDPERGSESFFYRQVLLALEQTDFCQFEVQFEITHNAIHSWTGGLTPYGMSTLEYTTYDPLFWLHHANTDRIWAIWQALQEYRGLPYDHANCEIQAMKRPLRPFSDPINHNAFTHSNAKPTDVFEYSRFNFQYDNLRFHGMTIKKLEHELEKQKEEDRTFAAFLLHGIKKSADVSFDVCNHDGECHFAGTFAILGGEHEMPWSFDRLFRYDITQVLKQMHLEYDSDFTFHMRIIDTSGKQLPSDLIKMPTVEHSPGGKHHEKHHEDHHEDILVRKNIHSLSHHEAEELRDALYKLQNDESHGGYEHIAGFHGYPNLCPEKGDEKYPCCVHGMSIFPHWHRLHTIQFERALKKHGSHLGIPYWDWTQTISSLPTFFADSGNNNPFFKYHIRSINQDTVRDVNEAIFQQTKFGEFSSIFYLALQALEEDNYCDFEVQYEILHNEVHALIGGAEKYSMSTLEYSAFDPYFMIHHASLDKIWIIWQELQKRRVKPAHAGSCAGDIMHVPLHPFNYESVNNDDFTRENSLPNAVVDSHRFNYKYDNLNLHGHNIEELEEVLRSLRLKSRVFAGFVLSGIRTTAVVKVYIKSGTDSDDEYAGSFVILGGAKEMPWAYERLYRFDITETVHNLNLTDDHVKFRFDLKKYDHTELDASVLPAPIIVRRPNNAVFDIIEIPIGKDVNLPPKVVVKRGTKIMFMSVDEAVTTPMLNLGSYTAMFKCKVPPFSFHAFELGKMYSVESGDYFMTASTTELCNDNNLRIHVHVDDE
Enzyme Length 3414
Uniprot Accession Number Q10583
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. {ECO:0000305|PubMed:8829804}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Cross-link (9); Disulfide bond (23); Erroneous gene model prediction (2); Glycosylation (6); Metal binding (51); Region (8); Repeat (7); Sequence conflict (1); Signal peptide (1)
Keywords 3D-structure;Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Metal-binding;Oxygen transport;Repeat;Secreted;Signal;Thioether bond;Transport;WD repeat
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space.
Modified Residue
Post Translational Modification PTM: Probably N-glycosylated (Probable). Asn-1280 and Asn-2484 are buried deeply in the protein which make them inaccessible for sugar attachment (Probable). Asn-3278 N-glycan is likely to represent a diantennate carbohydrate tree (Probable). The didecamer is almost evenly tagged by a total of 120 sugar trees (Probable). {ECO:0000305|PubMed:19013468}.
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2); Electron microscopy (1)
Cross Reference PDB 3L6W; 3QJO; 4BED;
Mapped Pubmed ID 23454609;
Motif
Gene Encoded By
Mass 392,246
Kinetics
Metal Binding METAL 17; /note="Divalent metal cation; structural"; /evidence="ECO:0000305|PubMed:19013468"; METAL 58; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 76; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 85; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 195; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 199; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 226; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 478; /note="Copper 3; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 498; /note="Copper 3; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 507; /note="Copper 3; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 618; /note="Copper 4; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 622; /note="Copper 4; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 649; /note="Copper 4; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 737; /note="Divalent metal cation; structural"; /evidence="ECO:0000305|PubMed:19013468"; METAL 892; /note="Copper 5; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 912; /note="Copper 5; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 921; /note="Copper 5; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1031; /note="Copper 6; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1035; /note="Copper 6; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1062; /note="Copper 6; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1309; /note="Copper 7; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1327; /note="Copper 7; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1336; /note="Copper 7; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1440; /note="Copper 8; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1444; /note="Copper 8; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1471; /note="Copper 8; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1721; /note="Copper 9; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1741; /note="Copper 9; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1750; /note="Copper 9; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1863; /note="Copper 10; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1867; /note="Copper 10; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 1894; /note="Copper 10; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2138; /note="Copper 11; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2157; /note="Copper 11; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2166; /note="Copper 11; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2276; /note="Copper 12; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2280; /note="Copper 12; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2307; /note="Copper 12; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2424; /note="Divalent metal cation; structural"; /evidence="ECO:0000305|PubMed:19013468"; METAL 2558; /note="Copper 13; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2577; /note="Copper 13; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2586; /note="Copper 13; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2686; /note="Copper 14; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2690; /note="Copper 14; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2717; /note="Copper 14; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 2962; /note="Copper 15; via tele nitrogen"; /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"; METAL 2981; /note="Copper 15; via tele nitrogen"; /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"; METAL 2990; /note="Copper 15; via tele nitrogen"; /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"; METAL 3091; /note="Copper 16; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 3095; /note="Copper 16; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"; METAL 3122; /note="Copper 16; via tele nitrogen"; /evidence="ECO:0007744|PDB:4BED"
Rhea ID
Cross Reference Brenda