位置:首页 > 蛋白库 > HOXM_AZOVI
HOXM_AZOVI
ID   HOXM_AZOVI              Reviewed;         207 AA.
AC   P40591;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Hydrogenase expression/formation protein HoxM;
GN   Name=hoxM;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=1624446; DOI=10.1128/jb.174.14.4549-4557.1992;
RA   Menon A., Mortenson L.E., Robson R.L.;
RT   "Nucleotide sequences and genetic analysis of hydrogen oxidation (hox)
RT   genes in Azotobacter vinelandii.";
RL   J. Bacteriol. 174:4549-4557(1992).
CC   -!- FUNCTION: Not known. Could be involved in the processing of
CC       hydrogenase.
CC   -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M80522; AAA22126.1; -; Genomic_DNA.
DR   EMBL; L23970; AAA19501.1; -; Unassigned_DNA.
DR   PIR; A44915; A44915.
DR   RefSeq; WP_012703497.1; NZ_FPKM01000029.1.
DR   AlphaFoldDB; P40591; -.
DR   SMR; P40591; -.
DR   MEROPS; A31.002; -.
DR   OMA; MGAKKMS; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016485; P:protein processing; IEA:InterPro.
DR   Gene3D; 3.40.50.1450; -; 1.
DR   InterPro; IPR004419; Pept_A31_hyd_express.
DR   InterPro; IPR023430; Pept_HybD-like_dom_sf.
DR   InterPro; IPR000671; Peptidase_A31.
DR   PANTHER; PTHR30302; PTHR30302; 1.
DR   Pfam; PF01750; HycI; 1.
DR   PRINTS; PR00446; HYDRGNUPTAKE.
DR   SUPFAM; SSF53163; SSF53163; 1.
DR   TIGRFAMs; TIGR00140; hupD; 1.
DR   TIGRFAMs; TIGR00072; hydrog_prot; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Hydrolase; Metal-binding; Nickel; Protease.
FT   CHAIN           1..207
FT                   /note="Hydrogenase expression/formation protein HoxM"
FT                   /id="PRO_0000201937"
FT   BINDING         19
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  22769 MW;  809A69FDFEE0F26C CRC64;
     MTAPNILILG IGNLLWADEG FGVRCVELLN ERYRFPDGVR LMDGGTQGIY LVQHVQQADC
     LIVFDAVDYG LAPGTLKIVR DDEVPRFMGA KRMSLHQTGF QDVLALAAFS GAYPRELLLI
     GVQPEELEDF GGSLREPVRA QLEPALRVAL EFLAERGVVA AARDGDAERL APAPLALGRY
     EAGRPAEELA YRHGDIRFIP QQPLEDD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024