HYPD_CUPNH
ID HYPD_CUPNH Reviewed; 379 AA.
AC P31903;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hydrogenase maturation factor HypD {ECO:0000250|UniProtKB:P24192};
GN Name=hypD; OrderedLocusNames=PHG016;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8352644; DOI=10.1007/bf00249034;
RA Dernedde J., Eitinger M., Friedrich B.;
RT "Analysis of a pleiotropic gene region involved in formation of
RT catalytically active hydrogenases in Alcaligenes eutrophus H16.";
RL Arch. Microbiol. 159:545-553(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Involved
CC in the biosynthesis of the Fe(CN)(2)CO cofactor.
CC {ECO:0000250|UniProtKB:P24192}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P24192};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000250|UniProtKB:P24192}.
CC -!- SIMILARITY: Belongs to the HypD family. {ECO:0000305}.
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DR EMBL; X70183; CAA49734.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85772.1; -; Genomic_DNA.
DR PIR; S29978; S29978.
DR RefSeq; WP_011153941.1; NZ_CP039289.1.
DR AlphaFoldDB; P31903; -.
DR SMR; P31903; -.
DR IntAct; P31903; 2.
DR STRING; 381666.PHG016; -.
DR EnsemblBacteria; AAP85772; AAP85772; PHG016.
DR GeneID; 39976702; -.
DR KEGG; reh:PHG016; -.
DR PATRIC; fig|381666.6.peg.12; -.
DR eggNOG; COG0409; Bacteria.
DR HOGENOM; CLU_048562_1_0_4; -.
DR OMA; MRYLDEY; -.
DR OrthoDB; 666873at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11740; -; 2.
DR Gene3D; 6.10.20.100; -; 1.
DR InterPro; IPR002780; Hyd_form_HypD.
DR InterPro; IPR042243; HypD_1.
DR InterPro; IPR042244; HypD_2_sf.
DR PANTHER; PTHR30149; PTHR30149; 1.
DR Pfam; PF01924; HypD; 1.
DR PIRSF; PIRSF005622; Hydrgn_mat_hypD; 1.
DR TIGRFAMs; TIGR00075; hypD; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Plasmid; Reference proteome.
FT CHAIN 1..379
FT /note="Hydrogenase maturation factor HypD"
FT /id="PRO_0000201446"
FT BINDING 36
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P24192"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P24192"
FT BINDING 67
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P24192"
SQ SEQUENCE 379 AA; 41907 MW; 510401FAAA6AB224 CRC64;
MKYIEEFRDG ELAQRIAAHV RAEARPGQRY NFMEFCGGHT HAISRYGVTE LLPENVRMIH
GPGCPVCVLP IGRIDLALHL ALERDAIVCT YGDTMRVPAS GGMSLIRAKA HGADIRMVYS
AADALKIAQR HPQREVVFLA IGFETTTPPT ALIIREAKAR QVDNFSVLCC HVLTPSAITH
ILESPEVRDY GTVPIDGFVG PAHVSIVIGT RPYEHFSREY GKPVVIAGFE PLDVMQAILM
LVRQVNSGRA EVENEFVRAV TRDGNESAQA MVSEVFELRP SFEWRGLGEV PYSALRIRAQ
FARFDAEQRF DLRYRPVPDN KACECGAILR GVKKPTDCKL FATVCTPENP MGSCMVSSEG
ACAAHYSYGR FKDIPLVAA