ID F8AIA0_PYRYC Unreviewed; 772 AA.
AC F8AIA0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=PYCH_06490 {ECO:0000313|EMBL:AEH24337.1};
OS Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH24337.1, ECO:0000313|Proteomes:UP000008386};
RN [1] {ECO:0000313|EMBL:AEH24337.1, ECO:0000313|Proteomes:UP000008386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX PubMed=21705594; DOI=10.1128/JB.05345-11;
RA Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT archaeon Pyrococcus yayanosii CH1.";
RL J. Bacteriol. 193:4297-4298(2011).
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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DR EMBL; CP002779; AEH24337.1; -; Genomic_DNA.
DR RefSeq; WP_013905394.1; NC_015680.1.
DR AlphaFoldDB; F8AIA0; -.
DR STRING; 529709.PYCH_06490; -.
DR GeneID; 10837225; -.
DR KEGG; pya:PYCH_06490; -.
DR eggNOG; arCOG01187; Archaea.
DR HOGENOM; CLU_009164_0_0_2; -.
DR OrthoDB; 371970at2157; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000008386; 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; IPR043129; ATPase_NBD.
DR InterPro; IPR004421; Carbamoyltransferase_HypF.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000905; Gcp-like_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; PF00814; TsaD; 1.
DR Pfam; PF07503; zf-HYPF; 2.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 200..386
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 772 AA; 86971 MW; 98572612B0543BAC CRC64;
MRAYRIKVQG IVQAVGFRPF VYRIAHAHNL RGYVRNLGDA GVEIVVEGRE EDIEAFLRDL
YTRKPPLARI DRLERKEIPP QGFDRFYIEK SSQEGEGGNS IIPPDIAICE DCLRELFDPA
NKRYMYPFIV CTNCGPRFTI IEDLPYDREN TTMKEFSMCD FCESEYKDPL NRRYHAEPVC
CPVCGPSYRL YTNDGQEITG DPLKKAAKLI DKGYIVAIKG IGGIHLACDA TREDIVAELR
RRTFRPQKPF AIMARDLETV KSFAYVSPEE EEELMSYRRP IIALRKKDPF PLPDNLAPGL
HTIGVMLPYA ATHYLLFHHS KTPVYVMTSA NYPGKPMVKD NEEAFKELRE IADYFLLHNR
KILNRADDSV VRFVDGKRAV IRRSRGFVPL PIEIPFEYNG LAVGAELMNA FGIAKGGKVY
PSQYIGNTSK VEVLEFMREA IAHFRRILRV KELDLIVADL HPSYNTTKLA MEIANELNVE
FLQVQHHYAH VASVMAEHGL EEVVGIALDG VGYGTDGKVW GGEVIYLGYE DVERLAHIAY
YPLPGGDIAS YYPLRALMGI LSKVYDVEEL EGIIRGYCPR AIESLKYGET EFKVALGQLV
RGINVAYASS TGRVLDALAV LLNVVYRRHY EGEPAMKLES FAMKGKNDLK LEVPVEGKTI
KVEELFVDVL DLLEKASPAD IAYSVHIAMA RTFAEVAVEK AREFGVKAVA LSGGVAYNEL
ITKTIRKIVE ANGLRFYSTY EVPRGDNGIN VGQAFLGGLY LEGYLSRDDL TM
//
