HYPB_AZOVI
ID HYPB_AZOVI Reviewed; 303 AA.
AC P31880;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN Name=hypB;
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=1610901; DOI=10.1016/0167-4781(92)90077-d;
RA Chen J.C., Mortenson L.E.;
RT "Identification of six open reading frames from a region of the Azotobacter
RT vinelandii genome likely involved in dihydrogen metabolism.";
RL Biochim. Biophys. Acta 1131:199-202(1992).
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; X63650; CAA45184.1; -; Genomic_DNA.
DR EMBL; L23970; AAA19509.1; -; Unassigned_DNA.
DR PIR; S23440; S23440.
DR RefSeq; WP_012703489.1; NZ_FPKM01000029.1.
DR AlphaFoldDB; P31880; -.
DR SMR; P31880; -.
DR OMA; GRSCHLD; -.
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; 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 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..303
FT /note="Hydrogenase maturation factor HypB"
FT /id="PRO_0000201436"
FT REGION 18..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..260
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 159
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 160
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 191
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
SQ SEQUENCE 303 AA; 33186 MW; 743E6775527D1922 CRC64;
MCTVCGCAEG ETRIEGEHHH HGHDHHHHEH PFVRRPAPAE AAPPAAGGPN LHFGQGPARA
HAPGLSQSRM LRIEQDILGK NDRYAAENRA RFEALSLFVL NLVSSPGSGK TSLLTRTIEL
LGRRRPLAVI EGDQQTDHDA ARIRATGVPA VQINTGKGCH LDAHMVGHAL ARLDDLEGGL
LFIENVGNLV CPAAFDLGEA HKVAILSVTE GEDKPLKYPD MFHAADLMLL NKTDLLPHLD
FDVEACIAYA RRVNPDIEVI RVSARSGEGM GEWLAWIERQ RGTRLRARID ALREQARALE
ALL