FIXI_RHILV
ID FIXI_RHILV Reviewed; 761 AA.
AC O33533;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nitrogen fixation protein FixI;
DE AltName: Full=E1-E2 type cation ATPase FixI;
DE EC=7.2.2.-;
GN Name=fixI;
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VF39;
RA Mitsch M.J., Rochepeau P., Hynes M.F.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: FixI is a pump of a specific cation involved in symbiotic
CC nitrogen fixation. The four proteins FixG, FixH, FixI, and FixS may
CC participate in a membrane-bound complex coupling the FixI cation pump
CC with a redox process catalyzed by FixG.
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AJ001522; CAA04807.1; -; Genomic_DNA.
DR AlphaFoldDB; O33533; -.
DR SMR; O33533; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..761
FT /note="Nitrogen fixation protein FixI"
FT /id="PRO_0000046155"
FT TOPO_DOM 1..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..716
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..106
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 453
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 50
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 637
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 641
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 761 AA; 80617 MW; 68B2EA8BD13B0D4B CRC64;
MSCCTMDAES VLALSTTSFS AEEVRLASQP LGEGLRQLDL SVSDVHCGGC ISTIERALLT
LPFVKTARVN LTARRVTCVY QEEIEARATD PSKILGEINS AGYRAHLFTP SAPESDKTRN
QLLLAIGVSG FAAPNIMLLS VSVWSGADAA TRDMFHWISA MIAAPALVYA GRFFFKSAWN
ALRHGRTNMD VPISVTVSLS YAVSLWETVH HGEHAWFDAS VSLLFFLLIG RTLDHIMREK
ARAAINGLAR LAPRGALLIN PDGSRRYIAV EEIAAGDEIS IAAGERVPVD GIVVSGESDL
DLSIVTGESS PVTVASDSEV SSGAMNLTGS LVLRATRIAK NSLLSEIIGL MEAAEGGRAR
YRRIADRAAT LYSPVVHLLA LVSFLAWGFL GGDWKQAMLV AVAVLIITCP CALGLAVPVV
QVVAAGELFR KGIMVKDGSA LERLAETDTV AFDKTGTLTM GSSRLVRVDA MDESAAAIAR
GLAAHSRHPL SRALVRDTET APISFDRVTE IPGGGLEARN GADIYRLGNA AFACGTSFVP
RTADSPFSEV VLSKNGVDLA RFFFDDTLRP GACEAIDRLD AAGLETLIVS GDRQTVVDNT
AHALGIDRAL GSLTPKQKVE ECQRLNGEGR RVLMVGDGIN DAPALAAAHV SMAPATASDI
GRQAADLVFF IDRLDAVPEA IAVARRSASL IRQNFALAIG YNVLAVPIAI AGLATPLIAA
VAMSTSSIIV VTNALRLNGF GKRPDMHIRR GIGRSAEVKA A
