ID H2C1B8_9CREN Unreviewed; 743 AA.
AC H2C1B8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=MetMK1DRAFT_00005410 {ECO:0000313|EMBL:EHP70039.1};
OS Metallosphaera yellowstonensis MK1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=671065 {ECO:0000313|EMBL:EHP70039.1, ECO:0000313|Proteomes:UP000003980};
RN [1] {ECO:0000313|EMBL:EHP70039.1, ECO:0000313|Proteomes:UP000003980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:EHP70039.1,
RC ECO:0000313|Proteomes:UP000003980};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Kozubal M., Macur R.E., Jay Z., Inskeep W., Woyke T.;
RT "Improved High-Quality Draft sequence of Metallosphaera yellowstonensis
RT MK1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; JH597761; EHP70039.1; -; Genomic_DNA.
DR AlphaFoldDB; H2C1B8; -.
DR STRING; 671065.MetMK1DRAFT_00005410; -.
DR eggNOG; arCOG01187; Archaea.
DR HOGENOM; CLU_009164_0_0_2; -.
DR OrthoDB; 371970at2157; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000003980; Unassembled WGS sequence.
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; 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; 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; SSF53067; Actin-like ATPase domain; 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:UP000003980};
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 743 AA; 82871 MW; F7BA421C4070E3A1 CRC64;
MQTLRIVVSG LVQGVGFRPF IYRIATESNV KGFVRNMGGS EVEIVIQGGK REISTFFSLF
YLKLPAPARI ESLRVEGLEE CKFGEFRIMP SSLDRREPSQ IPPDFTVCDD CLREVLDQRN
RRYRYPFNSC AYCGPRFSMI MAIPYDRENT SMRDFPLCEH CSGEYSNPTD ERRFDAQGIS
CPICGPRLFL EDLSGERVEG DPILQTAKLL SEGHIVAVKG VGGYHIAVNP FNDDLVKELR
RRKNRPEKPF AVMSISTSVV SRYAYLSREE VEALESPERP IVLLRKREES QLSKYISPGL
DREGFFLYYT PLHYLILREV EGNSLIMTSG NKHGYPMCID EKCVREKLKG IADYVLYHNR
QIVNRVDDSV MKFTGSRRHL LRRGRGFAPL WIRLRRIGLP GLAIGAELGN AGGVLLGDKA
ILTQYVGDTD RVDNLVQLER SLDFLLRTYG VAPKVVITDK NPAYQSRRLA RKYAERFSAQ
LVEVQHHFAH ALSVSAERGV EEGIAITIDG VGYGDDGNAW GGEILRFRGA DYSREFHLRY
IPYPGGDVNA LKPRRMLANF LGTFMDWEEA GKVAGIPPEE VVVLSNLNRR PGLLTSSTGR
FLDAVSAYLG VCHRRTYEGE PAIKLEAAAK GGKVLDLDLP VRGREIDTVE AFKWLVSHDP
PLADAAATVL YRLGEALVKA ALRLNPDVIL VSGGAAVNEY ILKGMEDNSQ GIRVVTPSKV
PAGDGGIALG QLNFSTLANL EGL
//
