(data stored in SCRATCH zone)

SWISSPROT: Q13HK4_PARXL

ID   Q13HK4_PARXL            Unreviewed;       812 AA.
AC   Q13HK4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=Bxe_C0535 {ECO:0000313|EMBL:ABE36435.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36435.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36435.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36435.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along
CC       with HypE, it catalyzes the synthesis of the CN ligands of the
CC       active site iron of [NiFe]-hydrogenases. HypF functions as a
CC       carbamoyl transferase using carbamoylphosphate as a substrate and
CC       transferring the carboxamido moiety in an ATP-dependent reaction
CC       to the thiolate of the C-terminal cysteine of HypE yielding a
CC       protein-S-carboxamide. {ECO:0000256|PIRNR:PIRNR006256}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) +
CC         phosphate; Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:59918; EC=3.6.1.7; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00520};
CC   -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC       {ECO:0000256|PIRNR:PIRNR006256}.
CC   -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC       {ECO:0000256|PIRNR:PIRNR006256}.
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DR   EMBL; CP000272; ABE36435.1; -; Genomic_DNA.
DR   RefSeq; WP_011493691.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0535; -.
DR   EnsemblBacteria; ABE36435; ABE36435; Bxe_C0535.
DR   GeneID; 4010049; -.
DR   KEGG; bxe:Bxe_C0535; -.
DR   PATRIC; fig|266265.5.peg.8295; -.
DR   eggNOG; ENOG4105C8H; Bacteria.
DR   eggNOG; COG0068; LUCA.
DR   HOGENOM; HOG000278743; -.
DR   KO; K04656; -.
DR   OMA; VQHHYAH; -.
DR   OrthoDB; 48295at2; -.
DR   BioCyc; BXEN266265:BXE_RS39195-MONOMER; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046944; P:protein carbamoylation; IEA:UniProtKB-UniRule.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   InterPro; IPR004421; Carbamoyltransferase_HypF.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR041440; HypF_C.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   InterPro; IPR011125; Znf_HypF.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   Pfam; PF17788; HypF_C; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   Pfam; PF07503; zf-HYPF; 2.
DR   PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00143; hypF; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13HK4.
DR   SWISS-2DPAGE; Q13HK4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       20    108       Acylphosphatase-like.
FT                                {ECO:0000259|PROSITE:PS51160}.
FT   DOMAIN      216    403       YrdC-like. {ECO:0000259|PROSITE:PS51163}.
FT   ACT_SITE     35     35       {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT   ACT_SITE     53     53       {ECO:0000256|PROSITE-ProRule:PRU00520}.
SQ   SEQUENCE   812 AA;  87325 MW;  DC95CE6FFE959897 CRC64;
     MPTRVHTVRD DEPLVSKWGG EAIRVRGLVQ GVGFRPAVWR LAHDCGVSGT VCNDGEGVLI
     RAWADRPVLE RFVAGLHGRC PPLGRIDSVE RRAVPDVAPA PGEFTIVESG GGPAHTGVVP
     DAVTCRACLD ETLDPSGRRY RYPFTNCTHC GPRLSIVGAI PYDRCATTMA AFPLCGACRR
     EYDDPGDRRF HAQAVACPAC GPRIWIEQAD GSRERGDPLE VACRYLRLGG IVAIKGLGGF
     QLACMATAQA AVTKLRVLKH RARKPFALLA RDVTMAERYC SVSNADAALL RSAAGPIVIM
     PAIGRTTAAD LSGVAPGTAT LGFMLPSTPL HHLIMRALDA PIVLTSGNVA DEPQCTANDD
     ARIRLAGMAD VFLMHDREIA SRIDDSVARV LHGVPRLLRS SRGYAPAPLR MPHDFAAAPP
     VLAMGAQQKN AFCLLREGEA LVSHHIGELE NGETYRDYKA SLARYEKLFG HDARVVAVDL
     HPEYLSRKLG IDIARQRSLP LAEIQHHHAH FAACLAENDI GLASNILGVV LDGHGMGTDR
     RLWGGEFLLG GYVDCTRVAS LTPVALPGGM RAVLEPWRNT YAHLRASLGW EWVARRYAKL
     DLVRFLAGRP LALLEQMIEG GVNSPVSSSA GRLFDAVAAA AGVCRERVQY EGQAAIEFEA
     LIDRRTLHDE DDALAYPFRI GEASDAAYPL LIDAKPMWLA LLDDLMRATP APVIAARFHK
     GFTIAIVQMV KRALGSRLHG SAPAVRTVAL SGGVMQNAAL FEQLSERLAA CGLVVLAHRQ
     VPANDGGIAL GQAAIAAGRA LAHVEQRNTL CA
//

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