HYPE_BRADU
ID HYPE_BRADU Reviewed; 346 AA.
AC P31906;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 3.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Carbamoyl dehydratase HypE {ECO:0000250|UniProtKB:P24193};
DE EC=4.2.1.- {ECO:0000250|UniProtKB:P24193};
DE AltName: Full=Hydrogenase maturation factor HypE {ECO:0000250|UniProtKB:P24193};
GN Name=hypE; OrderedLocusNames=bll6927;
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=CB1809;
RX PubMed=8510650; DOI=10.1007/bf00281623;
RA van Soom C., Verreth C., Sampaio M.J., Vanderleyden J.;
RT "Identification of a potential transcriptional regulator of hydrogenase
RT activity in free-living Bradyrhizobium japonicum strains.";
RL Mol. Gen. Genet. 239:235-240(1993).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=7906310; DOI=10.1006/jmbi.1994.1149;
RA Garg R.P., Menon A.L., Jacobs K., Robson R.M., Robson R.L.;
RT "The hypE gene completes the gene cluster for H2-oxidation in Azotobacter
RT vinelandii.";
RL J. Mol. Biol. 236:390-396(1994).
RN [3]
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: Involved in the maturation of [NiFe] hydrogenases. Along with
CC HypF, it catalyzes the synthesis of the CN ligands of the active site
CC iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent
CC dehydration of the carboxamido group attached to its C-terminal
CC cysteine to a cyano group. {ECO:0000250|UniProtKB:P24193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] =
CC ADP + C-terminal S-cyanate-L-cysteinyl-[HypE protein] + H(+) +
CC phosphate; Xref=Rhea:RHEA:55644, Rhea:RHEA-COMP:14247, Rhea:RHEA-
CC COMP:14248, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:139126, ChEBI:CHEBI:139127, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P24193};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000250|UniProtKB:P24193}.
CC -!- PTM: Modified by HypF, which adds a carboxamido group to the thiolate
CC of the C-terminal cysteine, yielding a protein-S-carboxamide. The
CC carboxamido group is then dehydrated by HypE itself to yield a protein-
CC thiocyanate. {ECO:0000250|UniProtKB:P24193}.
CC -!- SIMILARITY: Belongs to the HypE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78989.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z17373; CAA78989.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000040; BAC52192.1; -; Genomic_DNA.
DR RefSeq; NP_773567.1; NC_004463.1.
DR RefSeq; WP_011089665.1; NZ_CP011360.1.
DR AlphaFoldDB; P31906; -.
DR SMR; P31906; -.
DR STRING; 224911.27355208; -.
DR EnsemblBacteria; BAC52192; BAC52192; BAC52192.
DR GeneID; 64026683; -.
DR KEGG; bja:bll6927; -.
DR PATRIC; fig|224911.44.peg.6961; -.
DR eggNOG; COG0309; Bacteria.
DR HOGENOM; CLU_049733_0_0_5; -.
DR InParanoid; P31906; -.
DR OMA; CGNGGKE; -.
DR PhylomeDB; P31906; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046892; P:peptidyl-S-carbamoyl-L-cysteine dehydration; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR CDD; cd02197; HypE; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR InterPro; IPR011854; HypE.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR PANTHER; PTHR30303; PTHR30303; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF005644; Hdrgns_mtr_HypE; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR02124; hypE; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..346
FT /note="Carbamoyl dehydratase HypE"
FT /id="PRO_0000201458"
FT MOD_RES 346
FT /note="S-carbamoylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P24193"
FT MOD_RES 346
FT /note="S-cyanocysteine"
FT /evidence="ECO:0000250|UniProtKB:P24193"
FT CONFLICT 21
FT /note="S -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 36296 MW; 2A2275713E717BDC CRC64;
MKAYQRKLDI RNGCVDLSHG SGGRAMAQLI SGLFHEAFGN EWLARGNDQS AFDVRAGRMV
MTTDGYVVSP LFFPGGNIGS LAVHGTVNDI AMAGAKPLYL SASFIIEEGF RFADLKLIAE
SMGAAAREAD VHIITGDTKV VERGKADGLF ISTAGVGVVP DGLDLSAEKA RVGDRVLISG
TLGDHGVAIM SKRQNLAFET EIVSDSASLH DLVARMVQAG GRGIRLMRDP TRGGLAATLN
EIAQQSNLGF HLLEEAIPVK PGVAAACELL GLDPLHVANE GKLVAIVAPE AAGAVLAAMR
AHPLGRDAAD IGEAVADDHH FVQMATSFGG GRIVDWLSGE QLPRIC
