HYPB_AZOCH
ID HYPB_AZOCH Reviewed; 305 AA.
AC Q43949;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN Name=hypB; Synonyms=hupB;
OS Azotobacter chroococcum mcd 1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8486288; DOI=10.1016/0378-1119(93)90616-b;
RA Tibelius K.H., Du L., Tito D., Stejskal F.;
RT "The Azotobacter chroococcum hydrogenase gene cluster: sequences and
RT genetic analysis of four accessory genes, hupA, hupB, hupY and hupC.";
RL Gene 127:53-61(1993).
RN [2]
RP ERRATUM OF PUBMED:8486288.
RA Tibelius K.H., Du L., Tito D., Stejskal F.;
RL Gene 134:141-141(1993).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC for nickel insertion into the metal center of the hydrogenase. Exhibits
CC a low intrinsic GTPase activity, which is essential for nickel
CC insertion. {ECO:0000250|UniProtKB:P0AAN3}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. HypB/HupM
CC subfamily. {ECO:0000305}.
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DR EMBL; L00674; AAA22133.1; -; Genomic_DNA.
DR PIR; JN0647; JN0647.
DR AlphaFoldDB; Q43949; -.
DR SMR; Q43949; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR CDD; cd05390; HypB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR004392; Hyd_mat_HypB.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30134; PTHR30134; 1.
DR Pfam; PF02492; cobW; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00073; hypB; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Metal-binding; Nickel; Nucleotide-binding; Zinc.
FT CHAIN 1..305
FT /note="Hydrogenase maturation factor HypB"
FT /id="PRO_0000201435"
FT REGION 101..262
FT /note="G-domain"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 2
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 5
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 7
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 161
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 162
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 193
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
SQ SEQUENCE 305 AA; 33345 MW; ACEA9196CEDE1E94 CRC64;
MCTVCGCAEG ETRIEGEHHH HGYDHGHHHH DHAFVRRPAP AEAAPLVVEG LNLHFGQGPA
RAHAPGLSQS RMVQIEQDIL GKNDRYAAEN RARFEALSLF VLNLVSSPGS GKTTLLTKTI
ELLGRHRPLA VIEGDQQTDH DAARIRATGV PAVQVNTGKG CHLDAHMVGR AFEQLEGLDG
GLLFIENVGN LVCPAAFDLG EAHKVAILSV TEGEDKPLKY PDMFHAADLM LLNKTDLLPH
LDFDVEACIA YARRVNPDIK VIRVSARSGE GMGEWLAWIE RQRGARLRAR IDALRAQAQA
LEALL
