HYPF_METJA
ID HYPF_METJA Reviewed; 766 AA.
AC Q58123;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Probable carbamoyltransferase HypF {ECO:0000250|UniProtKB:P30131};
DE EC=6.2.-.- {ECO:0000250|UniProtKB:P30131};
DE AltName: Full=Carbamoyl phosphate-converting enzyme HypF;
DE AltName: Full=[NiFe]-hydrogenase maturation factor HypF;
DE Short=Hydrogenase maturation protein HypF;
GN Name=hypF; OrderedLocusNames=MJ0713;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC HypE, it catalyzes the synthesis of the CN ligands of the active site
CC iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase
CC using carbamoylphosphate as a substrate and transferring the
CC carboxamido moiety in an ATP-dependent reaction to the thiolate of the
CC C-terminal cysteine of HypE yielding a protein-S-carboxamide.
CC {ECO:0000250|UniProtKB:P30131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl
CC phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE
CC protein] + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:55636,
CC Rhea:RHEA-COMP:14247, Rhea:RHEA-COMP:14392, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:76913,
CC ChEBI:CHEBI:139126, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P30131};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000250|UniProtKB:P30131}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98708.1; -; Genomic_DNA.
DR PIR; A64389; A64389.
DR AlphaFoldDB; Q58123; -.
DR SMR; Q58123; -.
DR STRING; 243232.MJ_0713; -.
DR EnsemblBacteria; AAB98708; AAB98708; MJ_0713.
DR KEGG; mja:MJ_0713; -.
DR eggNOG; arCOG01187; Archaea.
DR HOGENOM; CLU_009164_0_0_2; -.
DR InParanoid; Q58123; -.
DR OMA; VQHHYAH; -.
DR PhylomeDB; Q58123; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046944; P:protein carbamoylation; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR043129; ATPase_NBD.
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; SSF53067; SSF53067; 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;
KW Ligase; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..766
FT /note="Probable carbamoyltransferase HypF"
FT /id="PRO_0000071619"
FT DOMAIN 11..98
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT DOMAIN 209..393
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT ZN_FING 117..142
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
FT ZN_FING 167..192
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
SQ SEQUENCE 766 AA; 87605 MW; 1B81EAB8D16CBFAD CRC64;
MEILFFGVKM KVRIKVKGIV QGVGFRPFVY RIAKKNNLKG YVKNMGNYVE ILIEGKKEDI
RNFINDLKNK KPPLSRIDKL DIEEIKGIEE FDDFYIIKSE NAKDEEEGTI PADVAICDDC
LKEMLDKNDR RYRYPFIACT NCGPRFTIVE KLPYDRENTS MRDFPLCEKC LEEYKNPLDR
RFHAQATCCP ICGPKVFLSD GKEIIAEKDE AIRETVKLLE EGHILAIKGI GGTHLACKVG
EDDVVLELRK RLGRPTQPFA VMSKIEYTEL FAEFDEDEKN ALLSLRRPIV VLKKSQDYDK
YFSKYVSNLD TIGVMFPYSG LHYLLFDKEI AYVMTSANLP GLPMVKDNDE ILKKLNGIAD
YFLLHNRRIV NRCDDSVVKK VADRLVFLRR SRGFAPEPVK VNINNNKNIL CVGAELNSTA
CIVKRDKFYL TQYIGNTSKY ETFCYLRDAI NNILRLTNTN KIDAIVCDLH PQFNSTKLAE
ELSEKFGAEI FRVQHHFAHA YSLLGDNNYF DDAIILSLDG VGYGLDGNIW GGEVLLFKDG
KMERVGHLEE QYQLGGDLAT KYPLRMLLSI LYKAIGEEAF DFIKRYNFFS EKELRLLKFQ
LEKKLNCPIT TSTGRVLDAV SALLGICFEK TYDGEPSIRL EPVANRFKGD INIEPKIKNN
ILNTTELIYK SYEMLLNNEN KEKIAHFAHI YIADGLFEIA KKISNKFGIN TIGITGGVSY
NKIITERIMN NAKREGFNFI YHQRVPNGDG GISFGQGVAY ILKNGY
