ID A0A109FE55_9BASI Unreviewed; 1756 AA.
AC A0A109FE55;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=RHOSPDRAFT_29930 {ECO:0000313|EMBL:KWU42834.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU42834.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU42834.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU42834.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004943}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family.
CC {ECO:0000256|ARBA:ARBA00007718}.
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DR EMBL; KQ954500; KWU42834.1; -; Genomic_DNA.
DR STRING; 1305733.A0A109FE55; -.
DR OrthoDB; 6047at2759; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
DR CDD; cd07542; P-type_ATPase_cation; 1.
DR Gene3D; 3.40.50.1400; -; 2.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_00323; Ferrochelatase; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR019772; Ferrochelatase_AS.
DR InterPro; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00109; hemH; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF53800; Chelatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS00534; FERROCHELATASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362082};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362082};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 422..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 634..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 670..691
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1180..1199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1205..1224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1245..1267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1293..1311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1323..1340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1360..1389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1410..1432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 216..371
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 1205..1376
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 193398 MW; D341651914F10296 CRC64;
METTPASILK PDRPYDPSAD ADLQFFPQEQ HVNTQEDATP EDPTAAGDED DYDDPDGALW
SGPAARSVPT SVSGRTTDAE SESDEVGFFE GLSNVLRGRS ASNARRGSSP SRTRPSLHSR
SSFADDAVSL TSEDPYGPYG STSEEDDDTR SDTSSSSSLE RRGGLPGMTG HAGDFFGESR
IDFEDDDEMS SISESSDGGD EPGGPMCHQL VYIVDEDLPL RFVGLHLSRW WLALWYLGCV
VTAGGLWLVG RWLPNLWRKA TGEMEIFAES DYVVVESHHH AAQILPLQTL KLPHPVPLGT
LFPPSVQIPP AHREDAATAA NNTPDNASVD EASINGNGAV PKKSSKFKAG GGPAVEELNF
IDYRYYRFLL HPDGMFRMVR DWKDPSWTSI AALRQGLSTE TDLAFRKTLF DSNAIEIEAK
GIGALLMDEV LHPFYIFQIF SIALWSVDDY YYYAFAIAVI SIVSIISTLL ETRANVERMR
EMSRFSCPVR VYRDSEWTID DSASLVPGDL IDLAYENLHT FPADVVLLSG DAIVNESMLT
GESVPVSKVP IESGVVSLVS APGGEIKADL SKHVLYNGTK IIRIRKTSPG GKGELEAVAM
VLRTGFNTTK GALVRSMLFP KPFGFAFYRD SFRFIGVLGM VAVLGFCASS VNFVRLGIAW
STIVIRALDL ITIVVPPALP ATMAIGTSFA IQRLRKQGIF CISPTRVNIG GKVSIVCFDK
TGTLTEEGLD VLGVRSVVRS ANVFTELHRD PDDVPIFGAA DAKTPLLHAL ATCHALKVVN
GEVIGDPLDL RMFEFTGWTL EEGKEGVGKR KTTAGTSSKV PERAQTLVQT VVRPPGGESF
KLEDALKAGK KHAHFLELGV LRTFDFVSSL RRMSVLVKKL KSTSVEVYVK GAPEVMIDIC
DKSTLPSDYD EILADYTKRG FRVIALAGKS MAGLTWIKAQ RLKRDAVESD LRFLGLVIFE
NKLKPGTAPA IATFRSAHIP TRMVTGDNVR TAISVGRECG MVQPLAQVYL PTFTQGGPSQ
PRSQIEWTDV DDETRTLDSY SLKPMVERDD RSVYSAYERE PQEYHLAVTG DVFRWMMDFG
ALETLQRMLV KGIIFARMSP DEKHELVERL QTLGYTVGFC GDGANDCGAL KAADVGLSLS
EAEASVAAPF TSRQPDIRCF LEVIKEGRAS LVTSFSCFKF MALYSLIQFT TVSLLYSIAS
TLGDFQFLYI DLFLILPIAV TMGRTEPYPR IHPKRPTANL ISKKVLTSLI GQIAITSAFQ
FFIFFFVRAQ SWYTAPTIDP EQLDIESYEN TSLFLISSFQ YILVAAVFCV GPPYRKPLYS
NRWLVLALVG LSTFSIYTLF MPPTSPVFGL LQFVDLPHDF HLELLLILLA NVALSWIFED
VGAQALARWI GDMQRRYRRM RGRRKESGKA YKAISRILIP LPFQSVLAPL IAKRRTPKIE
KQYAAIGGGS PILKWTRIQG KGMAELLDEL SPETAPHKAY VAFRYANPKT ETCLEEMKRD
GVKRAIAFTQ YPQYSCSTTG SSLNELYRQV GEAAPKGKET AAQDDIQWSV IDRWGVHPGF
VDSVARNIEA SLATYPASSR DKVVLLFSAH SLPMSVVNRG DPYPAEVAAS VSAIMARLGN
RNPYRLVWQS QVGPSAWLGP QTSDAIKGYA KKGLNDLLLV PVAFTSDHIE TLFELDLEYL
EEAKELCMTG VKRVESLNDS PYFIRAIADI AAAHLKSGQA VSAQMGLRCP GCTNERCGKQ
KEWFEGFQGK IAAPAA
//
