ID C1D517_LARHH Unreviewed; 794 AA.
AC C1D517;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:ACO73834.1};
GN OrderedLocusNames=LHK_00841 {ECO:0000313|EMBL:ACO73834.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO73834.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO73834.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO73834.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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:0000256|PIRNR:PIRNR006256}.
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:0000256|ARBA:ARBA00001186,
CC ECO:0000256|PIRNR:PIRNR006256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711, ECO:0000256|PIRNR:PIRNR006256}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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DR EMBL; CP001154; ACO73834.1; -; Genomic_DNA.
DR RefSeq; WP_012696326.1; NC_012559.1.
DR AlphaFoldDB; C1D517; -.
DR STRING; 557598.LHK_00841; -.
DR KEGG; lhk:LHK_00841; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_4; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000002010; Chromosome.
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:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.90.870.50; -; 1.
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; Sua5-like_dom.
DR InterPro; IPR011125; Znf_HypF.
DR NCBIfam; TIGR00143; hypF; 1.
DR PANTHER; PTHR42959; CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR42959:SF1; CARBAMOYLTRANSFERASE HYPF; 1.
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; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 23..110
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 218..418
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 794 AA; 86531 MW; EECA788E726E7440 CRC64;
MPAASAPSFE VPDLTSHEEA VHCEQWLLRG LVQGVGFRPF VWQLARRLGI QGQIRNTGEG
VEILAQGQPA RLAAFERALH EERPPLAEFE LTARQSLPAD PALGDFSIGS SQESGHGATI
PPDIATCPEC LRELFTPADR RHRYPFINCT HCGPRYTITR QLPYDRAQTS MAAFGLCPLC
QHEYLDPSSR RFHAEPIACP VCGPQLRLTD RFAVPLKGDP VTGTLQFLRM GRCVAIKGLG
GFHLACNARS AEAVARLRML KHRPSRPLAV MALNLASVET FCHVSPEEAA LLQSPKRPIV
LLQKRAEADQ YLPGIAPGMN TVGVMLPYTP IHWLMFHESL RRPAGLDWME APCADVWVMT
SANLSGEPIV TDNDDARHRL NTVADAFLIH NRQVAARCDD SLMMMIDHEP HLLRRARGFA
PAPLALRHDG ATVLAVGGPD KNTVTLLRGT QALVSPHIGG LDHPLTCETH NSAIRHLERW
ANAEPGCIAC DLDPDNHASQ HAEQLAGLRQ LPLLRIQRHH ALVSAVLAEH DVDVPVLGLV
MDGGGTGADG NEWGGELLRV HGVSMERLAH LPHIPLPGGE RASREPWRVA AGWLIRNGLG
DEAARRYGRE PSFVELSEQV THQLRCPDSS SSSRWFDAIA SLAGLCSRQS FSSEARLRLE
ALARPVAPLA GGWRLDDNGQ LDWSPVVHHL LTLTDAEEIA SLWHASCAAA VAEWVIRHAR
QQQIDHVVLA GSSCSNRVLQ QALHRHLLQA GLTLLESRQL PSGAGALSLG QACVARQWLA
GRASGTVPAI GVTG
//
