ID L5JMB5_PTEAL Unreviewed; 1089 AA.
AC L5JMB5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ferroxidase {ECO:0000256|ARBA:ARBA00013107};
DE EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
GN ORFNames=PAL_GLEAN10016335 {ECO:0000313|EMBL:ELK00544.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK00544.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001830};
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KB031157; ELK00544.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JMB5; -.
DR STRING; 9402.L5JMB5; -.
DR eggNOG; KOG1263; Eukaryota.
DR InParanoid; L5JMB5; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR CDD; cd11021; CuRO_2_ceruloplasmin; 1.
DR CDD; cd04224; CuRO_3_ceruloplasmin; 1.
DR CDD; cd11022; CuRO_4_ceruloplasmin; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR024715; Factor_5/8-like.
DR PANTHER; PTHR46806:SF7; COAGULATION FACTOR VIII; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR PIRSF; PIRSF000354; Factors_V_VIII; 3.
DR SUPFAM; SSF49503; Cupredoxins; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000354-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1089
FT /note="ferroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003968306"
FT DOMAIN 91..199
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 222..357
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 968..1072
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DISULFID 174..200
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 276..357
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 535..561
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 638..719
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1089 AA; 125364 MW; 519F3A5768F1E616 CRC64;
MKILLLGTFL FLYNITARAK DKHYYIGIIE TTWNYASDNG EKKLISVDTE HSNIYLQNGP
NRIGRLYKKA LYLQYTDDTF ETTVEKPVWL GFLGPIIKAE TGDKVYVHLK NFASRPYTFH
SHGITYYKEN EGAIYPDNTT DFHKADDKVY PGDQYTYVLH ASQEQSPGEE DGNCVTRIYH
SHIDAPRDIA SGLIGPLIFC KKGSLEEEKE KNIDQEFVVM FSVVDENFSW YLDDNIKTYC
SEPEKADKDD KDFQESNKMY SVNGYAFGSL PGLSMCAEDR VKWYIFGMGN EIDVHAAYFH
GQTLTNKNYR IDTINLFPAT LFDAFMVAQN PGEWMLSCQN LNHLKAGLQA FFQVRDCNKP
SSEDDIRGKH VRHYYIAAEE IIWNYAPSGI DTFTNEKLTA PESASEVFFE HGRTRIGGSY
KKLVYREYTD ASFTNQKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKAA YPLSIEPTGV
RVNKSNEGTY YSSHYSSQSG SVPSPSASHV APKETFTYEW TIPKEVGPTY KDPVCLSKMY
YSAVDPTKDI FTGLIGPMKI CKKGSLHANG RQKDIDKEFY LFPTVFDENE SLLLDDNIKM
FTTSPDQVDK EDADFQESNK MHSMNGFMYG NQPGLNMCQG DSVVWYLFSA GNEADVHGIY
FSGNTYLSKG ERRDTANLFP QTSLTLFMQP DTEGTFDVEC LTTDHYTGGM KQNYTVNQCR
QLSKNPNLYL GERTYYIAAV EVEWDYSPSR EWEKELHHLQ EQNVSNVFFD KEEFFIGSKY
KKVVYLQYTD SMFQVPVERK AEEEHLGILV CLKGKFLKTI LSTLLFKTNY PDISSFWVTG
YQDLGYMCPI YTKYNQIHQH LINLGETRTY IWKIPERSGA GNEDSACIPW AYYSTVDQVK
DLYSGLIGPL IVCRRHYMKV FNPIKKLEFF LLFFVFDENE SWYLDENIKT YSDHPEKVNK
DNDEFIESNK MHAINGRMFG NLQGLIMHAG DEVNWYLMGM GNEIDLHSVH FHGHSFQYKH
RGIYSSDVFD IFPGTYQTLE MFPRTPGIWL LHCHVTDHIH AGMETTYTVL PNEGEYQVSD
SRSLCHKYN
//
