FIXI_BRADU
ID FIXI_BRADU Reviewed; 730 AA.
AC Q59207;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Nitrogen fixation protein FixI;
DE AltName: Full=E1-E2 type cation ATPase FixI;
DE EC=7.2.2.-;
GN Name=fixI; OrderedLocusNames=blr2769;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=8661920; DOI=10.1007/s002030050330;
RA Preisig O., Zufferey R., Hennecke H.;
RT "The Bradyrhizobium japonicum fixGHIS genes are required for the formation
RT of the high-affinity cbb3-type cytochrome oxidase.";
RL Arch. Microbiol. 165:297-305(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; X95634; CAA64889.1; -; Genomic_DNA.
DR EMBL; AJ005001; CAA06285.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC48034.1; -; Genomic_DNA.
DR RefSeq; NP_769409.1; NC_004463.1.
DR RefSeq; WP_011085554.1; NZ_CP011360.1.
DR AlphaFoldDB; Q59207; -.
DR SMR; Q59207; -.
DR STRING; 224911.27351026; -.
DR EnsemblBacteria; BAC48034; BAC48034; BAC48034.
DR GeneID; 64022526; -.
DR KEGG; bja:blr2769; -.
DR PATRIC; fig|224911.44.peg.2390; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_5; -.
DR InParanoid; Q59207; -.
DR OMA; CKTVYEI; -.
DR PhylomeDB; Q59207; -.
DR Proteomes; UP000002526; Chromosome.
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; SSF81660; SSF81660; 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; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..730
FT /note="Nitrogen fixation protein FixI"
FT /id="PRO_0000046154"
FT TOPO_DOM 1..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..382
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..85
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 438
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 30
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 33
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 622
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 730 AA; 77339 MW; 41588689FE78AD25 CRC64;
MHVTRDFSHY VRTAGEGIKH IDLAVEGVHC AGCMAKIERG LSAIPDVTLA RVNLTDRRVA
LEWKAGTLDP GRFIDRLEEL GYKAYPFETE SAEVAEVAES RFLLRCLGVA AFATMNVMML
SIPVWSGNVS DMLPEQRDFF HWLSALIALP AAAYAGQPFF RSAWRALSAK TTNMDVPISI
GVILALGMSV VETIHHAEHA YFDAAIMLLT FLLVGRFLDQ NMRRRTRAVA GNLAALKAET
AAKFVGPDEI SQVPVAAISP GDIVLLRPGE RCAVDGTVIE GRSEIDQSLI TGETLYVTAE
QGTPVYAGSM NISGTLRVRV SAASEATLLA EIARLLDNAL QARSRYMRLA DRASRLYAPV
VHATALITIL GWVIAGASWH DAIVTGVAVL IITCPCALGL AIPTVQTVAS GAMFKSGVLL
NSGDAIERLA EADHVIFDKT GTLTLPDLEV MNAADIPADI FELAGRLALS SHHPVAAAVA
QAAGARSPIV GAVEEAGQGV RADVDGAEIR LGRPSFCGAE ALVGDGTRLD PEASIVAFSK
GAEKFILWVR QGLRPDAQAV IAALKARNIG IEILSGDREP AVKAAAHALA IPEWRAGVTP
ADKIARIEEL KRRGARVLMV GDGMNDAPSL AAAHVSMSPI SAAHLSQATA DLVFLGRPLA
PVAAAIDSAR KALHLMRQNL WLAIGYNVLA VPVAISGVVT PLIAAAAMSG SSILVMLNSL
RARSDSREIV
